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- EMDB-42226: High resolution in-situ structure of typeA supercomplex in respir... -

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Entry
Database: EMDB / ID: EMD-42226
TitleHigh resolution in-situ structure of typeA supercomplex in respiratory chain (I1III2IV1,composite)
Map dataIn-situ structure of supercomplex in respiratory chain ( typeA )
Sample
  • Complex: In-situ cryo-EM structure of respiratory supercomplex by directly imaging mitochondria
    • Protein or peptide: x 64 types
  • Protein or peptide: x 4 types
  • Ligand: x 25 types
Keywordsin-situ cryo-EM structure / mammalian / mitochondria / respiratory supercomplex / proton pumping / membrane protein / electron transport
Function / homology
Function and homology information


Cytoprotection by HMOX1 / TP53 Regulates Metabolic Genes / respiratory chain complex III / respiratory chain complex IV assembly / mitochondrial respirasome assembly / RHOG GTPase cycle / respiratory chain complex IV / deoxynucleoside kinase activity / Complex I biogenesis / Respiratory electron transport ...Cytoprotection by HMOX1 / TP53 Regulates Metabolic Genes / respiratory chain complex III / respiratory chain complex IV assembly / mitochondrial respirasome assembly / RHOG GTPase cycle / respiratory chain complex IV / deoxynucleoside kinase activity / Complex I biogenesis / Respiratory electron transport / Neutrophil degranulation / mitochondrial respiratory chain complex IV / regulation of oxidative phosphorylation / Mitochondrial protein degradation / mitochondrial respiratory chain complex III / cytochrome-c oxidase / cardiac muscle tissue development / mitochondrial respirasome / quinol-cytochrome-c reductase / ubiquinone-6 biosynthetic process / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, cytochrome c to oxygen / cellular respiration / oxidoreductase activity, acting on NAD(P)H / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / NADH dehydrogenase activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial ATP synthesis coupled electron transport / mitochondrial respiratory chain complex I / ubiquinone binding / mitochondrial electron transport, NADH to ubiquinone / mitochondrial respiratory chain complex I assembly / acyl binding / NADH dehydrogenase (ubiquinone) activity / acyl carrier activity / electron transport coupled proton transport / quinone binding / ATP synthesis coupled electron transport / enzyme regulator activity / negative regulation of intrinsic apoptotic signaling pathway / aerobic respiration / response to cAMP / respiratory electron transport chain / reactive oxygen species metabolic process / central nervous system development / electron transport chain / regulation of protein phosphorylation / brain development / mitochondrial intermembrane space / negative regulation of cell growth / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / NAD binding / positive regulation of fibroblast proliferation / FMN binding / nervous system development / 4 iron, 4 sulfur cluster binding / response to oxidative stress / mitochondrial inner membrane / membrane => GO:0016020 / electron transfer activity / oxidoreductase activity / nuclear body / mitochondrial matrix / copper ion binding / heme binding / protein-containing complex binding / mitochondrion / proteolysis / nucleoplasm / metal ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
NADH-ubiquinone reductase complex 1 MLRQ subunit / NADH-ubiquinone reductase complex 1 MLRQ subunit / Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Cytochrome c oxidase, subunit 8 / Cytochrome c oxidase, subunit 8 superfamily / Cytochrome oxidase c subunit VIII / Cytochrome c oxidase subunit VIIa, metazoa / Cytochrome C oxidase, subunit VIIB ...NADH-ubiquinone reductase complex 1 MLRQ subunit / NADH-ubiquinone reductase complex 1 MLRQ subunit / Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Cytochrome c oxidase, subunit 8 / Cytochrome c oxidase, subunit 8 superfamily / Cytochrome oxidase c subunit VIII / Cytochrome c oxidase subunit VIIa, metazoa / Cytochrome C oxidase, subunit VIIB / Cytochrome c oxidase subunit IV / Cytochrome C oxidase, subunit VIIB domain superfamily / Mitochondrial cytochrome c oxidase subunit VIc/VIIs / Cytochrome c oxidase, subunit VIIa superfamily / Mitochondrial cytochrome c oxidase subunit VIc/VIIs superfamily / Cytochrome c oxidase subunit VIc / Cytochrome C oxidase chain VIIB / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / : / Cytochrome c oxidase, subunit VIa, conserved site / Cytochrome c oxidase subunit VIa signature. / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV family / Globular protein, non-globular alpha/beta subunit / Cytochrome c oxidase subunit VIIc superfamily / Cytochrome c oxidase subunit IV superfamily / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV / Cytochrome c oxidase, subunit VIa / Cytochrome c oxidase, subunit Va/VI / Cytochrome b-c1 complex, subunit 6 / Cytochrome c oxidase, subunit VIa superfamily / Cytochrome c oxidase, subunit Va/VI superfamily / Cytochrome c oxidase subunit VIa / Cytochrome c oxidase subunit Va / Cytochrome c oxidase, subunit VIb / Cytochrome c oxidase, subunit VIb superfamily / Cytochrome oxidase c subunit VIb / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit 2, C-terminal / Cytochrome c oxidase subunit III domain / Cytochrome c oxidase subunit Vb, zinc binding region signature. / Cytochrome c oxidase, subunit Vb / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome c oxidase subunit Vb / Cytochrome c oxidase subunit Vb, zinc binding domain profile. / Cytochrome c oxidase subunit I domain / Cytochrome c oxidase, subunit II / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome c oxidase subunit III / Cytochrome c oxidase subunit III-like / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome c oxidase subunit III / Heme-copper oxidase subunit III family profile. / Cytochrome c oxidase subunit III-like superfamily / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome b / Cytochrome c/quinol oxidase subunit II / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / Cytochrome C oxidase subunit II, transmembrane domain superfamily / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / NADH-ubiquinone oxidoreductase 1 subunit C1 / NADH-ubiquinone oxidoreductase flavoprotein 3 / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH:ubiquinone oxidoreductase, ESSS subunit / ESSS subunit of NADH:ubiquinone oxidoreductase (complex I) / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature.
Similarity search - Domain/homology
NADH-ubiquinone oxidoreductase chain 1 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / Cytochrome b-c1 complex subunit 7 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / Cytochrome c oxidase subunit / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / Cytochrome c oxidase subunit 7B, mitochondrial / Cytochrome b-c1 complex subunit Rieske, mitochondrial / NADH dehydrogenase [ubiquinone] 1 subunit C2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 ...NADH-ubiquinone oxidoreductase chain 1 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / Cytochrome b-c1 complex subunit 7 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / Cytochrome c oxidase subunit / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / Cytochrome c oxidase subunit 7B, mitochondrial / Cytochrome b-c1 complex subunit Rieske, mitochondrial / NADH dehydrogenase [ubiquinone] 1 subunit C2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 / Cytochrome c oxidase subunit 4 / NADH:ubiquinone oxidoreductase subunit V3 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Cytochrome c oxidase subunit 6C / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / Cytochrome c1, heme protein, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 / Cytochrome b-c1 complex subunit 1, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / Cytochrome b-c1 complex subunit 8 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 / Complex III subunit 9 / Cytochrome b-c1 complex subunit 6 / Acyl carrier protein / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / Mitochondrial NDUFA4 / Cytochrome c oxidase subunit / Cytochrome c oxidase subunit 8 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / Cytochrome b-c1 complex subunit 10 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / Cytochrome c oxidase polypeptide Va / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH-ubiquinone oxidoreductase chain 2 / Cytochrome c oxidase subunit 1 / NADH-ubiquinone oxidoreductase chain 3 / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 6 / Cytochrome c oxidase subunit 2 / NADH-ubiquinone oxidoreductase chain 4L / Cytochrome b / Cytochrome c oxidase subunit 7C, mitochondrial / Cytochrome c oxidase subunit 3 / Cytochrome c oxidase subunit 5B, mitochondrial / Cytochrome c oxidase subunit 7A1, mitochondrial / NADH-ubiquinone oxidoreductase chain 5
Similarity search - Component
Biological speciesSus scrofa (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.1 Å
AuthorsZheng W / Zhang K / Zhu J
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R35GM142959 United States
CitationJournal: Nature / Year: 2024
Title: High-resolution in situ structures of mammalian respiratory supercomplexes.
Authors: Wan Zheng / Pengxin Chai / Jiapeng Zhu / Kai Zhang /
Abstract: Mitochondria play a pivotal part in ATP energy production through oxidative phosphorylation, which occurs within the inner membrane through a series of respiratory complexes. Despite extensive in ...Mitochondria play a pivotal part in ATP energy production through oxidative phosphorylation, which occurs within the inner membrane through a series of respiratory complexes. Despite extensive in vitro structural studies, determining the atomic details of their molecular mechanisms in physiological states remains a major challenge, primarily because of loss of the native environment during purification. Here we directly image porcine mitochondria using an in situ cryo-electron microscopy approach. This enables us to determine the structures of various high-order assemblies of respiratory supercomplexes in their native states. We identify four main supercomplex organizations: IIIIIV, IIIIIV, IIIIIV and IIIIIV, which potentially expand into higher-order arrays on the inner membranes. These diverse supercomplexes are largely formed by 'protein-lipids-protein' interactions, which in turn have a substantial impact on the local geometry of the surrounding membranes. Our in situ structures also capture numerous reactive intermediates within these respiratory supercomplexes, shedding light on the dynamic processes of the ubiquinone/ubiquinol exchange mechanism in complex I and the Q-cycle in complex III. Structural comparison of supercomplexes from mitochondria treated under different conditions indicates a possible correlation between conformational states of complexes I and III, probably in response to environmental changes. By preserving the native membrane environment, our approach enables structural studies of mitochondrial respiratory supercomplexes in reaction at high resolution across multiple scales, from atomic-level details to the broader subcellular context.
History
DepositionOct 5, 2023-
Header (metadata) releaseJun 19, 2024-
Map releaseJun 19, 2024-
UpdateJun 19, 2024-
Current statusJun 19, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_42226.png

Downloads & links

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Map

FileDownload / File: emd_42226.map.gz / Format: CCP4 / Size: 2.6 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationIn-situ structure of supercomplex in respiratory chain ( typeA )
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.42 Å/pix.
x 888 pix.
= 370.296 Å		0.42 Å/pix.
x 888 pix.
= 370.296 Å		0.42 Å/pix.
x 888 pix.
= 370.296 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.417 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.12
Minimum - Maximum-0.000000000274021 - 1.6322932
Average (Standard dev.)0.004740206 (±0.030185716)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions888888888
Spacing888888888
CellA=B=C: 370.296 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: In-situ structure of supercomplex in respiratory chain ( typeA )

Fileemd_42226_additional_1.map
AnnotationIn-situ structure of supercomplex in respiratory chain ( typeA )
Projections & Slices
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Additional map: In-situ structure of supercomplex in respiratory chain ( typeA )

Fileemd_42226_additional_2.map
AnnotationIn-situ structure of supercomplex in respiratory chain ( typeA )
Projections & Slices
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Additional map: In-situ structure of supercomplex in respiratory chain ( typeA )

Fileemd_42226_additional_3.map
AnnotationIn-situ structure of supercomplex in respiratory chain ( typeA )
Projections & Slices
AxesZYX

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Sample components

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Entire : In-situ cryo-EM structure of respiratory supercomplex by directly...

EntireName: In-situ cryo-EM structure of respiratory supercomplex by directly imaging mitochondria
Components
  • Complex: In-situ cryo-EM structure of respiratory supercomplex by directly imaging mitochondria
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 6
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4L
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 5
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
    • Protein or peptide: NADH:ubiquinone oxidoreductase subunit A9
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
    • Protein or peptide: NADH:ubiquinone oxidoreductase subunit AB1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 isoform X1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
    • Protein or peptide: NADH:ubiquinone oxidoreductase subunit A13
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 subunit C2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 [Sus scrofa]
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
    • Protein or peptide: NADH:ubiquinone oxidoreductase subunit B2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 1, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 2, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 7
    • Protein or peptide: Cytochrome b-c1 complex subunit 8
    • Protein or peptide: Cytochrome b-c1 complex subunit 6, mitochondrial
    • Protein or peptide: Ubiquinol-cytochrome c reductase complex 7.2 kDa protein
    • Protein or peptide: Cytochrome b-c1 complex subunit 10
    • Protein or peptide: Cytochrome c oxidase subunit 1
    • Protein or peptide: Cytochrome c oxidase subunit 2
    • Protein or peptide: Cytochrome c oxidase subunit 3
    • Protein or peptide: Cytochrome c oxidase subunit 4
    • Protein or peptide: Cytochrome c oxidase subunit 5A, mitochondrial
    • Protein or peptide: Cytochrome c oxidase subunit 5B, mitochondrial
    • Protein or peptide: Cytochrome c oxidase subunit 6A2
    • Protein or peptide: Cytochrome c oxidase subunit 6B1
    • Protein or peptide: Cytochrome c oxidase subunit 6C
    • Protein or peptide: Cytochrome c oxidase subunit 7A1, mitochondrial
    • Protein or peptide: Cytochrome c oxidase subunit 7B
    • Protein or peptide: Cytochrome c oxidase subunit 7C, mitochondrial
    • Protein or peptide: Cytochrome c oxidase subunit 8
    • Protein or peptide: Cytochrome c oxidase subunit NDUFA4
  • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
  • Protein or peptide: Cytochrome b
  • Protein or peptide: Cytochrome c1, heme protein, mitochondrial
  • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: POTASSIUM IONPotassium
  • Ligand: CARDIOLIPIN
  • Ligand: GUANOSINE-5'-TRIPHOSPHATEGuanosine triphosphate
  • Ligand: MAGNESIUM ION
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: ZINC ION
  • Ligand: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate
  • Ligand: N-ACETYLMETHIONINE
  • Ligand: MYRISTIC ACID
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: HEME C
  • Ligand: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE
  • Ligand: HEME-A
  • Ligand: COPPER (II) ION
  • Ligand: SODIUM IONSodium
  • Ligand: DINUCLEAR COPPER ION
  • Ligand: (7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-17,20-DIEN-1-AMINIUM 4-OXIDE
  • Ligand: (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)METHYL]ETHYL (5E,8E,11E,14E)-ICOSA-5,8,11,14-TETRAENOATE
  • Ligand: PHOSPHATE IONPhosphate
  • Ligand: water

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Supramolecule #1: In-situ cryo-EM structure of respiratory supercomplex by directly...

SupramoleculeName: In-situ cryo-EM structure of respiratory supercomplex by directly imaging mitochondria
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#39, #41-#46, #50-#68
Source (natural)Organism: Sus scrofa (pig)

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Macromolecule #1: NADH-ubiquinone oxidoreductase chain 3

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 3 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 13.026458 KDa
SequenceString:
(FME)NIMLTLLTN VTLASLLVLI AFWLPQLNAY SEKTSPYECG FDPMGSARLP FSMKFFLVAI TFLLFDLEIA LLLPLP WAS QTNNLKTMLT MALFLLILLA ASLAYEWTQK GLEWAE

UniProtKB: NADH-ubiquinone oxidoreductase chain 3

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Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 28.500184 KDa
SequenceString: MRNVSTQVPV SAHRPSRFGQ RPRIPGALQR TDRRGCLKAE AEMAALAASG LLRPILALRS SMGAAVQVRF VHPSAATDSP SSSQPAVSQ AGAVVSKPTT LPSSRGEYVV AKLDDLVNWA RRSSLWPMTF GLACCAVEMM HMAAPRYDMD RFGVVFRASP R QSDVMIVA ...String:
MRNVSTQVPV SAHRPSRFGQ RPRIPGALQR TDRRGCLKAE AEMAALAASG LLRPILALRS SMGAAVQVRF VHPSAATDSP SSSQPAVSQ AGAVVSKPTT LPSSRGEYVV AKLDDLVNWA RRSSLWPMTF GLACCAVEMM HMAAPRYDMD RFGVVFRASP R QSDVMIVA GTLTNKMAPA LRKVYDQMPE PRYVVSMGSC ANGGGYYHYS YSVVRGCDRI VPVDIYVPGC PPTAEALLYG IL QLQRKIK REKRLRIWYR R

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

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Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 30.154318 KDa
SequenceString: MAAAAAARGC WRGLVGPAAV ARVSGRPSVL LLPVRKESAA ADTRPTIRPR NDVVHKQLSA FGQYVAEILP KYVQQVQVSC FNELEIFIH PDGVIPVLTF LRDHTNAQFK SLADLTAVDV PTRQNRFEIV YNLLSLRFNS QIRVKTYTDE LTPIESSVTV Y KAANWYER ...String:
MAAAAAARGC WRGLVGPAAV ARVSGRPSVL LLPVRKESAA ADTRPTIRPR NDVVHKQLSA FGQYVAEILP KYVQQVQVSC FNELEIFIH PDGVIPVLTF LRDHTNAQFK SLADLTAVDV PTRQNRFEIV YNLLSLRFNS QIRVKTYTDE LTPIESSVTV Y KAANWYER EIWDMFGVFF ANHPDLRRIL TGYGFEGHPF RKDFPLSGYV ELRYDDEVKR VVAEPVELAQ EFRKFDLNSP WE AFPAYRQ PPEDLKLEAG DKKPETK

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

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Macromolecule #4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 54.168074 KDa
SequenceString: MAALRALCSL RGVAAQVLRP GAGARLPIQP SRGARQWQPD VEWAEQFGGA VMYPTKETAH WKPPPWNGNY YWPNYFPLLS DVDPPKDTL VSNLTLNFGP QHPAAHGVLR LVMELSGEMV RKCDPHIGLL HRGTEKLIEY KTYLQALPYF DRLDYVSMMC N EQAYSLAV ...String:
MAALRALCSL RGVAAQVLRP GAGARLPIQP SRGARQWQPD VEWAEQFGGA VMYPTKETAH WKPPPWNGNY YWPNYFPLLS DVDPPKDTL VSNLTLNFGP QHPAAHGVLR LVMELSGEMV RKCDPHIGLL HRGTEKLIEY KTYLQALPYF DRLDYVSMMC N EQAYSLAV EKLLNIQPPP RAQWIRVLFG EITRLLNHIM AVTTHALDIG AMTPFFWMFE EREKMFEFYE RVSGARMHAA YI RPGGVHQ DLPLGLLDDI YEFSKNFSFR IDELEEMLTN NRIWRNRTVD IGVVTAEDAL NYGFSGVMLR GSGIQWDLRK TQP YDVYDQ VEFDVPIGSR GDCYDRYLCR VEEMRQSLRI ISQCLNKMPP GEIKVDDAKV SPPKRAEMKT SMESLIHHFK LYTE GYQVP PGATYTAIEA PKGEFGVYLV SDGSSRPYRC KIKAPGFAHL AGLDKMSKGH MLADVVAIIG TQDIVFGEVD R

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

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Macromolecule #5: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 27.439533 KDa
SequenceString: MFLTAALRAR ATGFTAQWGR HVRNLHKTAV QNGAGGALFV HRDTPENNPD TPFDFTPENY KRIEAIVKNY PEGHKAAAVL PVLDLAQRQ NGWLPISAMN KVAEILQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK V GETTPDKL ...String:
MFLTAALRAR ATGFTAQWGR HVRNLHKTAV QNGAGGALFV HRDTPENNPD TPFDFTPENY KRIEAIVKNY PEGHKAAAVL PVLDLAQRQ NGWLPISAMN KVAEILQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK V GETTPDKL FTLIEVECLG ACVNAPMVQI NDNYYEDLTP KDIEEIIDEL KAGKIPKPGP RSGRFSCEPA GGLTSLTEPP KG PGFGVQA GL

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

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Macromolecule #6: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 50.637766 KDa
SequenceString: MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG DWYKTKEILL KGPDWILGEV KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IIRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN ...String:
MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG DWYKTKEILL KGPDWILGEV KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IIRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN LQVAIREAYE AGLIGKNACG SGYDFDVFVV RGAGAYICGE ETALIESIEG KQGKPRLKPP FPADVGVFGC PT TVANVET VAVSPTICRR GGAWFASFGR ERNSGTKLFN ISGHVNHPCT VEEEMSVPLK ELIEKHAGGV IGGWDNLLAV IPG GSSTPL IPKSVCETVL MDFDALVQAQ TGLGTAAVIV MDRSTDIVKA IARLIEFYKH ESCGQCTPCR EGVDWMNKVM ARFV KGDAR PAEIDSLWEI SKQIEGHTIC ALGDGAAWPV QGLIRHFRPE LEERMQQFAL QHQARQAAS

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

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Macromolecule #7: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

MacromoleculeName: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 79.627398 KDa
SequenceString: MLRIPVTRAL IGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL ...String:
MLRIPVTRAL IGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL VKTIMTRCIQ CTRCIRFASE IAGVDDLGTT GRGNDMQVGT YIEKMFMSEL SGNIIDICPV GALTSKPYAF TA RPWETRK TESIDVMDAV GSNIVVSTRT GEVMRILPRM HEDINEEWIS DKTRFAYDGL KRQRLTQPMI RNEKGLLTYT TWE DALSRV AGMLQSFQGN DVAAIAGGLV DAEALVALKD LLNRVDSDSL CTEEVFPTAG AGTDLRSNYL LNTTIAGVEE ADVI LLVGT NPRFEAPLFN ARIRKSWLHN DLKVALIGSP VDLTYRYDHL GDSPKILQDI ASGNHPFSQI LKEAKKPMVV LGSSA LQRS DGTAILAAVS NIAQNIRLSS GVTGDWKVMN ILHRIASQVA ALDLGYKPGV EAIRKNPPKV LFLLGADGGC ITRQDL PKD CFIIYQGHHG DVGAPMADVI LPGAAYTEKS ATYVNTEGRA QQTKVAVTPP GLAREDWKII RALSEIAGMT LPYDTLD QV RSRLEEVSPN LVRYDDVEGA NYFQQANELS KLVNQQLLAD PLVPPQLTIK DFYMTDSISR ASQTMAKCVK AVTEGIQA V EEPSIC

UniProtKB: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

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Macromolecule #8: NADH-ubiquinone oxidoreductase chain 1

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 1 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 35.619434 KDa
SequenceString: (FME)FMINILSLI IPILLAVAFL TLVERKVLGY MQLRKGPNVV GPYGLLQPIA DALKLVTKEP LRPGTSSISM FIIAPI LGL SLALTMWVPL PMPYPLINMN LGVLFMLAMS SLAVYSILWS GWASNSKYAL IGALRAVAQT ISYEVTLAII LLSVLLM NG SYTLSTLITT ...String:
(FME)FMINILSLI IPILLAVAFL TLVERKVLGY MQLRKGPNVV GPYGLLQPIA DALKLVTKEP LRPGTSSISM FIIAPI LGL SLALTMWVPL PMPYPLINMN LGVLFMLAMS SLAVYSILWS GWASNSKYAL IGALRAVAQT ISYEVTLAII LLSVLLM NG SYTLSTLITT QEHIWMIFTS WPLAMMWFIS TLAETNRAPF DLTEGESELV SGFNVEYAAG PFAMFFMAEY ANIIMMNA F TAILFLGASH DPHTPELYTI NFVLKTLALT ITFLWIRASY PRFRYDQLMH LLWKSFLPLT LALCMWHISL PIMTASIPP QS

UniProtKB: NADH-ubiquinone oxidoreductase chain 1

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Macromolecule #9: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 27.135039 KDa
SequenceString: MEASQECRLR LSVDRPPPHG KERQRFKMRC LSTPMLLRAL AQAQAAHAGH PSARTLHSSA VAATYKFVNM REPSMDMKSV TDRAAQTLL WTELVRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAV CPAQAITIEA E PRADGSRR ...String:
MEASQECRLR LSVDRPPPHG KERQRFKMRC LSTPMLLRAL AQAQAAHAGH PSARTLHSSA VAATYKFVNM REPSMDMKSV TDRAAQTLL WTELVRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAV CPAQAITIEA E PRADGSRR TTRYDIDMTK CIYCGFCQEA CPVDAIVEGP NFEFSTETHE ELLYNKEKLL NNGDKWEAEI AANIQADYLY R

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

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Macromolecule #10: NADH-ubiquinone oxidoreductase chain 6

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 6 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 19.021332 KDa
SequenceString:
MTMYIAFILS TIFVIGFVGF SSKPSPIYGG LGLIVSGGVG CGIVLNFGGS FLGLMVFLIY LGGMLVVFGY TTAMATEMYP EVWVSNKTV FGAFVSGLMM EFCMVYYALK EEEVEIIFKF NGLGDWVIYD TGDSGFFSEE AMGIAALYSY GTWLVIVTGW S LLIGVVVI MEITRGN

UniProtKB: NADH-ubiquinone oxidoreductase chain 6

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Macromolecule #11: NADH-ubiquinone oxidoreductase chain 4L

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4L / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 10.855263 KDa
SequenceString:
(FME)PLVYMNIIM AFAIALAGLL MYRSHLMSSL LCLEGMMLSL FIMSTLIILN THFTLANMMP IILLVFAACE AALGLS LLV MVSNTYGTDY VQNLNLLQC

UniProtKB: NADH-ubiquinone oxidoreductase chain 4L

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Macromolecule #12: NADH-ubiquinone oxidoreductase chain 5

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 5 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 68.723508 KDa
SequenceString: (FME)NPFASLTLT TLIILTIPIM MSNSNIYKTN LYPNYVKTTV SYAFTLSLVP LLMFMHTGQE MIISNWHWMT LQTVEL SLS FKMDYFSVMF IPVALFVTWS IMEFSMWYMH SDPFINRFFK YLVLFLITMM ILVTANNLFQ LFIGWEGVGI MSFLLIG WW HGRTDANTAA ...String:
(FME)NPFASLTLT TLIILTIPIM MSNSNIYKTN LYPNYVKTTV SYAFTLSLVP LLMFMHTGQE MIISNWHWMT LQTVEL SLS FKMDYFSVMF IPVALFVTWS IMEFSMWYMH SDPFINRFFK YLVLFLITMM ILVTANNLFQ LFIGWEGVGI MSFLLIG WW HGRTDANTAA LQAILYNRIG DIGFVLSMAW FLTHSNAWDL QQIFMLNNEC PNMPLIGLLL AAAGKSAQFG LHPWLPSA M EGPTPVSALL HSSTMVVAGV FLLIRFYPLM ETNKLVQTMT LCLGAITTLF TALCAITQND IKKIVAFSTS SQLGLMMVT IGINQPHLAF LHICMHAFFK AMLFMCSGSI IHSLNDEQDI RKMGGLYKAM PFTTTALIIG SLALTGMPYL TGFYSKDLII EAVNMSYTN AWALLMTLIA TSLTAAYSTR IIFFAFLGKP RFPPLVLINE NNPLLINSIK RLLIGSIFAG FIISNNIPPM T VPNTTMPL YMKMTALIVT IMGFMLALEL NNTTYYLKFK YPSQTYKFSN MLGYYPSIMH RLPTYHNLSM SQKSASSLLD LI WLETILP KTTSFIQMKM SIMVSNQKGL IKLYFLSFLI TIMISMTLFN YHE

UniProtKB: NADH-ubiquinone oxidoreductase chain 5

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Macromolecule #13: NADH-ubiquinone oxidoreductase chain 4

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 51.887395 KDa
SequenceString: (FME)LKIIIPTTM LLPMTWMSKH NMIWINATVH SLLISLISLS LLNQLGENSL NFSLTFFSDS LSAPLLVLTT WLLPLM LMA SQSHLSKETT TRKKLYITML ILLQLFLIMT FTATELILFY ILFEATLVPT LIIITRWGNQ TERLNAGLYF LFYTLAG SL PLLVALVYIQ ...String:
(FME)LKIIIPTTM LLPMTWMSKH NMIWINATVH SLLISLISLS LLNQLGENSL NFSLTFFSDS LSAPLLVLTT WLLPLM LMA SQSHLSKETT TRKKLYITML ILLQLFLIMT FTATELILFY ILFEATLVPT LIIITRWGNQ TERLNAGLYF LFYTLAG SL PLLVALVYIQ NTTGSLNFLI IHYWSHPLSN SWSNIFMWLA CIMAFMVKMP LYGLHLWLPK AHVEAPIAGS MVLAAVLL K LGGYGMMRIT TILNPLTNYM AYPFLMLSMW GMIMTSSICL RQTDLKSLIA YSSVSHMALV IVAIMIQTPW SFMGATALM IAHGLTSSML FCLANTNYER VHSRTMILAR GLQTLLPLMA TWWLMASLTN LALPPSINLI GELFIITASF SWSNITIILM GMNMMITAL YSLYMLITTQ RGKYTHHINN IKASFTRENA LMALHILPLL LLTLNPKMIL GPLY

UniProtKB: NADH-ubiquinone oxidoreductase chain 4

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Macromolecule #14: NADH-ubiquinone oxidoreductase chain 2

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 2 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 39.105512 KDa
SequenceString: (FME)NPIIYTTLI MTVMSGTMLV MISSHWLLIW IGFEMNLLAM IPVLMKNFNP RATEAATKYF LTQATASMML MMAIII NLL YSGQWTITKM FNPVAMTMMT MALAMKLGLS PFHFWVPEVT QGISLQAGLL LLTWQKLAPL SVLCQISQSI NPNLMLT MA MLSILIGGWG ...String:
(FME)NPIIYTTLI MTVMSGTMLV MISSHWLLIW IGFEMNLLAM IPVLMKNFNP RATEAATKYF LTQATASMML MMAIII NLL YSGQWTITKM FNPVAMTMMT MALAMKLGLS PFHFWVPEVT QGISLQAGLL LLTWQKLAPL SVLCQISQSI NPNLMLT MA MLSILIGGWG GLNQTQLRKI MAYSSIAHMG WMTAVLPYNT TMTILNLLIY ITMTLAMFML LIHSSATTTL SLSHTWNK M PVITSLMMVT LLSMGGLPPL SGFMPKWMII QEMTKNESII MPTLMAMTAL LNLYFYMRLA YSSSLTMFPS TNNMKMKWQ FEHTKQMKLL PTMIVLSTLV LPMTPALSSL N

UniProtKB: NADH-ubiquinone oxidoreductase chain 2

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Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 40.476082 KDa
SequenceString: MALRLLRLAP ASASAVPRGL GAVAQRVGGI HTGAPCRLQY GPLAFVLGER TTRKLTETSK VITVDGNICS GKGRLAREIA EKLGLRHFP EAGIHYADST TGDGKPLDVQ LSGNCSLEKF YDDPKSNDGN SYRLQSWLYA SRLLQYADAL EHLLSTGQGV V LERSIYSD ...String:
MALRLLRLAP ASASAVPRGL GAVAQRVGGI HTGAPCRLQY GPLAFVLGER TTRKLTETSK VITVDGNICS GKGRLAREIA EKLGLRHFP EAGIHYADST TGDGKPLDVQ LSGNCSLEKF YDDPKSNDGN SYRLQSWLYA SRLLQYADAL EHLLSTGQGV V LERSIYSD FVFLEAMYRQ GFIRKQCVEH YNEVKKVTAC EYLPPHVVVY VDVPVPEIQS RIQKKGNPHE MKITAAYLQD IE NAYKKTF LPEMSEKCEV LQYSAREAED AEKVVEDIEY LKCDKGPWPD QDDRTFHRLR MLVQNKLEVL NYTTIPVYLP EIT IGAHQS DRVFQKFTEL PGRKYSPGYN EDVGDKWIWL K

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial

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Macromolecule #16: NADH:ubiquinone oxidoreductase subunit A9

MacromoleculeName: NADH:ubiquinone oxidoreductase subunit A9 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 42.606324 KDa
SequenceString: MAAAVHPRVV RAVPMSRSCL AAVATSVSYG PPQRQLHHAL IPHGKGGRSS VSGIVATVFG ATGFLGRYVV NHLGRMGSQV IVPYRCEPY DTMHLRPMGD LGQIIFMEWN GKDKDSIRKV VEHSNVVINL VGREWETKNF DFEDVFVKIP HAIAQVSKEA G VEKLIHIS ...String:
MAAAVHPRVV RAVPMSRSCL AAVATSVSYG PPQRQLHHAL IPHGKGGRSS VSGIVATVFG ATGFLGRYVV NHLGRMGSQV IVPYRCEPY DTMHLRPMGD LGQIIFMEWN GKDKDSIRKV VEHSNVVINL VGREWETKNF DFEDVFVKIP HAIAQVSKEA G VEKLIHIS HLNADIKSPS RYLRSKAVGE KEVRAAFPEA TIIKPSDIFG REDRFLNYFA SMRWFGGVPL ISLGKETVKQ PV YIVDVSK GIINAIKDPD AKGKTFAFVG PNRYLLFDLV QYIFAVAYRP FLPYPLPHFA YRWVGRLFEV SPFEPWTTRD KVE RVHMSD MTLPHLPGLE DLGIQATPLE LKAIEVLRRH RTYRWLTSEM EDVKPAKTVN I

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

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Macromolecule #17: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 19.746514 KDa
SequenceString:
MAAVSMSVAL KQALWGRRAA AVGAVSVSKV PTRLLSTSTW RLAQDQTQDT QLIAVDEKLD ITTLTGVPEE HIKTRKVRIF VPARNNMQS GVNNTKKWKM EFDTRERWEN PLMGWSSTAD PLSNLVLTFS TKEDAVAFAE KNGWSFDVEE RKVPKPKSKS Y GANFSWNK RTRVSTK

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

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Macromolecule #18: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 13.34895 KDa
SequenceString:
MAAVTFLRLL GRSGAGARNL LGGSRCFGVR TSPTGEKVTH TGQAYDDGDY RRVRFSDRQK EVNENFAIDL IAEQPVSEVG SRVISCDGG GGALGHPRVY INLDKETKTG TCGYCGLQFR QPHH

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

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Macromolecule #19: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 11.099798 KDa
SequenceString:
MAAAAASRGI RAKLGLREIR IHLCQRSPGS QGVRDFIEKR YVELKKANPD LPILIRECSD VQPKLWARYA FGQEKNVSLN NFSADQVTR TLENVLSGKA

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

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Macromolecule #20: NADH:ubiquinone oxidoreductase subunit AB1

MacromoleculeName: NADH:ubiquinone oxidoreductase subunit AB1 / type: protein_or_peptide / ID: 20 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 17.338211 KDa
SequenceString:
MAARVLCACV RRLPAAFAPL PRIPTVVAAR PLSTTLFPTG AQARSRALQP ALVLAQAPSG VTQLCRRYSD APPLTLEAIK DRVLYVLKL YDKIDPEKLS VNSHFMKDLG LDSLDQVEII MAMEDEFGFE IPDIDAEKLM CPQEIVDYIA DKKDVYE

UniProtKB: Acyl carrier protein

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Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 isof...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 isoform X1
type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 13.32159 KDa
SequenceString:
MAGLLKKTTG LVGLAVCETP HERLKILYTK ILDVLGQIPK NAAYRKYTEQ ITNEKLGMVK AEPDVKKLEE QLQGGQIEEV ILQAENELS LARKMLRWKP WEPLVEEPPA NQWKWPI

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5

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Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.953313 KDa
SequenceString:
MAASGLPRAA AAAGTSVKPI FSRDMNEAKR RVRELYRAWY REVPNTVHLF QLDISVKQGR DKVREMFMKN AHVTDPRVVD LLVIKGKME LEETINVWKQ RTHIMRFFHE TEAPRPTDFL SKFYVGHDP

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

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Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 20.064096 KDa
SequenceString:
MPGIVELPTL EDLKVQEVKV SSSVLKAAAH HYGAQCDKPN KEFMLCRWEE KDPRRCLEEG KLVNQCALDF FRQIKRHCAE PFTEYWTCI DYSGLQLFRH CRKQQAKFDE CVLDKLGWVR PDLGELSKVT KVKTDRPLPE NPYHSRARPE PNPEAEGDLK P AKHGSRLF FWTM

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8

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Macromolecule #24: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.686894 KDa
SequenceString:
MAKTLLHKYS DIPEGTECHR KAYASTSIGG ATGLIVSAYS IALKPPASFL EGVARTGRYT FTSAAIGAIF GLTSCISAQV REKPDDPLN YFIGGCAGGL TLGARTRSYG IGAAACAYMG LTAALVKMGQ LEGWQVFAEP KV

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11

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Macromolecule #25: NADH:ubiquinone oxidoreductase subunit A13

MacromoleculeName: NADH:ubiquinone oxidoreductase subunit A13 / type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 16.911611 KDa
SequenceString:
MAASKVKQDM PPPGGYGPID YKRNLPRRGL SGYSMFAVGI GTLLFGYWSM MKWNRERRRL QIEDFEARIA LMPLFQAEKD RRVLQMLRE NLEEEAIIMK DVPDWKVGES VFHTTRWVTP MMGELYGLRT NEEILSATYG FIWYT

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

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Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 8.034373 KDa
SequenceString:
MWFEILPGIA VMAACLFIPG MATAHIHKFT NGGKEKRVAH FSYQWNLMER DRCISGVNRY HVTKGLENID

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1

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Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.225567 KDa
SequenceString:
MAGRIASFLK NAWAKEPVLV ASFAIGGLAI ILPSLSPYTN YAIRINRATP YNYPVPLRDD GNMPDVPSHP QDPQGPSLEW LKNL

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3

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Macromolecule #28: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
type: protein_or_peptide / ID: 28 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 8.664053 KDa
SequenceString:
MAASALFRPF SKLLSSARLP SGSSARSKFY IREPPHGSPD WLKVGLTLGT SVFLWIYLIK QHKEDVLEYK RRNGLE

UniProtKB: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial

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Macromolecule #29: NADH dehydrogenase [ubiquinone] 1 subunit C2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 subunit C2 / type: protein_or_peptide / ID: 29 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.327655 KDa
SequenceString:
MTMMSGRPGR VPLQFLPNEA RSLPPPKLTD PRLVYMGFLG YCSGLIDNAI RRRPVVSAGL HRQLLYVTSF VFFGYYLLKR QDYMYALRD HDMFAYVKSH PEDFPEKDKK TYGEILEEFH PVR

UniProtKB: NADH dehydrogenase [ubiquinone] 1 subunit C2

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Macromolecule #30: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / type: protein_or_peptide / ID: 30 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.506591 KDa
SequenceString:
MPFFDVQKRL GLDLDRWMTI QSAEQPHKIP GRCHAFEKEW IECAHGIGGI RAEKECKIEF DDFVECLLRQ KTMKRLSAIK RQRDKLIKE GKYTPPPHHL GKEDPRP

UniProtKB: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

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Macromolecule #31: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 [Sus ...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 [Sus scrofa]
type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 15.371934 KDa
SequenceString:
MAAAILKLEE TRGGGEKCDK NQGVKGRRFM ISRSHPSLRA GPANGRSRGH SFRRRWWLGS PLPLVVGVVV GSEAAAFMMN VLQIVRDHW VHILVPVGFV FGCYLDRRSD EKLTAFRNKS LLFKRELRPN EEVTWK

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1

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Macromolecule #32: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial
type: protein_or_peptide / ID: 32 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 17.384729 KDa
SequenceString:
MAAGVLGLCA RRLLAAAATR GLPAARVRWE SGSSRAVIAP SALVGKRPPE PTIRLQEDPD PEDENLYEKN PDSHGYDKDP IVDLWNMRV VFFFGFSIVL VLGSTFVAYL PDYRMQEWAR REAERLVKYR EANGLPLMES NCFDPNKIQL PEDED

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial

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Macromolecule #33: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
type: protein_or_peptide / ID: 33 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 21.587006 KDa
SequenceString:
MAAMSLLQRA SVTAVATLSR SRLGTRFGFG GFLTHGFPKT GAPVRHSGDH GKRLFIIKPS GFYDRRFLKL MRFYILLTGI PVAIGITLV NVFIGEAELA DIPEGYVPEH WEYFKHPISR WIARTFYDGP EKNYEKTMAI LQIEAEKAEL RLKELEVRRL M RARGDGPW YQYPTIDKAL IDHSPKTTPD N

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial

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Macromolecule #34: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
type: protein_or_peptide / ID: 34 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 15.645212 KDa
SequenceString:
M(SAC)GYTPDEKL RLQQLRELRR RWLKDQELSP REPVLPPRRV WPMEQFWNKF LQDGAPWKNV IYKTYRHSIF AVTHVL IPV WIIHYYLKYH VTAKPYTVVE RKPRIFPGDT ILETGEVIPL MKEFPDQHH

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6

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Macromolecule #35: NADH:ubiquinone oxidoreductase subunit B2

MacromoleculeName: NADH:ubiquinone oxidoreductase subunit B2 / type: protein_or_peptide / ID: 35 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 11.939366 KDa
SequenceString:
MSPLQRLAPF TRVGGRFLRG RGAGVAGGGG VRHAGGGVHI EPRYRQFPQL TRSQLIQAEF FSATMWFWIL WRFWHDSDAV LGHFPYPDP SQWTDEELGI LPDDED

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial

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Macromolecule #36: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
type: protein_or_peptide / ID: 36 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 11.128515 KDa
SequenceString:
MAHGHGHEHG HSKMELPDYK QWKIEGTPLE TVQEKLAARG LRDPWGRNEA WRYSGGFANN VSFVGALLKG FKWGFAAFVV AVGAEYYLE SQNKDKKHH

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3

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Macromolecule #37: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 21.658447 KDa
SequenceString:
MASAKAGVLG VRWLQRAARK VVPLGARTAS HVTKDMFPGP YPKTPEERAA AAKKYNMRVE DYEPYPDDGM GYGDYPKLPD RSQQERDPW YDWDHPDLRL NWGEPIHWDL DMYIRNRVDT SPTPVSWNTM CKHLSGFVAF MLFMFWVGEI YPSYQPVGPK Q YPYNDLYL ERGGDPTKEP EPVVHYEI

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial

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Macromolecule #38: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
type: protein_or_peptide / ID: 38 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 15.11735 KDa
SequenceString:
MSFPKYKPSR LATLPATLDP AEYDISPETR KAQAERLAIR SRLKREYLLQ YNDPNRLGVI EDPALIRWTY ARSANIYPNF RPTPKTSLL GALFGIGPLF FWYYVFKTDR DKKEKLIQEG KLDQTFNISY

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

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Macromolecule #39: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
type: protein_or_peptide / ID: 39 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 21.864906 KDa
SequenceString:
MAFSAPAAYL THQQKVLRLY KRALRHLESW CVHRDKYRYF ACLMRARFDE HKNEKDMVKA TQLLRQAEEE FWYGQHPQPY IFPESPGGT SYERYECYKV PEWCLDDWHP SEKAMYPDYF AKREQWKRLR RESWEREVKQ LQEETPPGGP RTEALPPARK E GDLPPLWW HIVTRPRERP M

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9

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Macromolecule #40: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
type: protein_or_peptide / ID: 40 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 16.567047 KDa
SequenceString:
(MYR)GAHLARRYL GDASKEPDPL RMPTFPPDYG FPERKEREMV ATQQEMNDAQ LMLQQRDYCA HYLIQLLKCK RDSFPN FLA CKHEQHDWDY CEHLDYVKRM KEFERERRLL QRKKRREQRE AEMARGQGPG EVAPEMAL

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

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Macromolecule #41: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
type: protein_or_peptide / ID: 41 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 20.944768 KDa
SequenceString:
MPDSWDKDVY PEPPRRTPAP APQTSLPNPV TYLTKIFDLL VDRPVTLARE FIEQQHAKNR YYYYHREFRR VPDITECEEK DILCMFEAE MQWRRDYKVD QEIVNIIQER LKACQQREGE SYRQNCAKEL EQFTQVSKAF QDRYSDLGAH YSARKCLAKQ K QRMLAERK AAKEAAAA

UniProtKB: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10

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Macromolecule #42: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 42 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 17.162439 KDa
SequenceString:
MELVQVLRRG LQQVSGHGGL RGYLRVLFRA NDVRVGTLVG EDKYGNKYYE DNKQFFGRHR WVIYTTEMNG RDTFWDVDGS MVPPEWHRW LHCMTDDPPT TKPPTARKYI WTNHKFNVSG TPQQYVPYST TRKKIQEWVP PSTPYK

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

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Macromolecule #43: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
type: protein_or_peptide / ID: 43 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.64859 KDa
SequenceString:
MASATRVIQL LRNWASGRDL QAKLQLRYQE ISKRTQPPPK LPVGPSHKLS NNYYCTRDGR REAMPPSIVM SSQKVLASGK PAESSAVAE TEKKAVTPAP PIKRWELSKD QPYL

UniProtKB: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7

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Macromolecule #44: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
type: protein_or_peptide / ID: 44 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 48.217836 KDa
SequenceString: MAASLLLRQG RARALKTVLL EGGVFRGLAP AVSLSAESGR NEKERPPNPK KQSPPKNVVA AQEGGTPLAT PAAPELSQQL SSPTSPPAA ARPGGTLAPP NPGDSTLFTD RGRPRFPSRK TLVEFPRKVL SPFSQQGSDS AATQASRGRA GDATSSSSSS S SSDSESDD ...String:
MAASLLLRQG RARALKTVLL EGGVFRGLAP AVSLSAESGR NEKERPPNPK KQSPPKNVVA AQEGGTPLAT PAAPELSQQL SSPTSPPAA ARPGGTLAPP NPGDSTLFTD RGRPRFPSRK TLVEFPRKVL SPFSQQGSDS AATQASRGRA GDATSSSSSS S SSDSESDD EEEGDGSEAV RPVKSTSPGG SPKAEAPRSL AGGAPQTGVP AEARPGPQQP HPDLAAAERP RQAKGKGGSG AP EDRRAPK AAAPGSRGGP GAARQSETPS QKIPRSEEAD AESQKPPEVK TSLPDPTKSG LSTAPRGGPA SAEPAATPAG ARL PATPLE TGERPLGERV PEPGGQVASP LFSRAPLGGQ AAEGVAEAKG ELLEGRPLVQ GPKAVPDGQD EGAEKKALRP EEEA GIAGD AAPGTAGRDA TQEPTPAAAA AEPFDNSTYR NLQHHEYSTY TFLDLNVELS KFRMPQPSSG RQSPRH

UniProtKB: NADH:ubiquinone oxidoreductase subunit V3

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Macromolecule #45: Cytochrome b-c1 complex subunit 1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 1, mitochondrial / type: protein_or_peptide / ID: 45 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 52.75632 KDa
SequenceString: MAASAVCRVA GTGSRVLLRT CRSPALLRSP ALRGTATYAQ ALQSVPETQV SQLDNGLRVA SEQSSQPTCT VGVWIDAGSR YENEKNNGA GYFVEHLAFK GTKNRPGSAL EKEVESMGAH LNAYSTREHT AYYIKALSKD LPKAVELLAD IVQNCSLEDS Q IEKERDVI ...String:
MAASAVCRVA GTGSRVLLRT CRSPALLRSP ALRGTATYAQ ALQSVPETQV SQLDNGLRVA SEQSSQPTCT VGVWIDAGSR YENEKNNGA GYFVEHLAFK GTKNRPGSAL EKEVESMGAH LNAYSTREHT AYYIKALSKD LPKAVELLAD IVQNCSLEDS Q IEKERDVI LQELQENDSS MRDVVFDYLH ATAFQGTPLA QSVEGPSENV RKLSRADLTE YVSQHYKAPR MVLAAAGGVE HR QLLDLAQ KHFSSLSGTY VEDAVPAFTP CRFTGSEIRH RDDALPLAHV AIAVEGPGWA NPDNVPLQVA NAIIGHYDST YGG GTHMSS TLASVAATRK LCQSFQTFNI CYAETGLLGA HFVCDNMSID DMMFFLQGQW MRLCTSATES EVVRGKNILR NALV SHLDG TTPVCEDIGR SLLTYGRRIP LAEWESRIAE VDASVVREVC SKYFYDQCPA VAGLGPIEQL PDYNRIRSGM FWLRF

UniProtKB: Cytochrome b-c1 complex subunit 1, mitochondrial

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Macromolecule #46: Cytochrome b-c1 complex subunit 2, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 2, mitochondrial / type: protein_or_peptide / ID: 46 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 48.262434 KDa
SequenceString: MKLITRAGSF SRFYSLKVAP KALASAAPAG VPLQPQDLEF TRLPNGLVIA SLENYAPASR IGLFIKAGSR YEDSNNLGTS HLLRLASSL TTKGASSFKI TRGIEAVGGK LSVTSTRESM AYTVECLRDD IEILMEFLLN VTAAPEFRRW EVAALQSQLR I DKAVAFQN ...String:
MKLITRAGSF SRFYSLKVAP KALASAAPAG VPLQPQDLEF TRLPNGLVIA SLENYAPASR IGLFIKAGSR YEDSNNLGTS HLLRLASSL TTKGASSFKI TRGIEAVGGK LSVTSTRESM AYTVECLRDD IEILMEFLLN VTAAPEFRRW EVAALQSQLR I DKAVAFQN PQAQVLENLH AAAYRNALAN SLYCPDYRIG KVTPDQLHYY VQNHFTSARM ALIGLGVSHP VLKQVAERFL NM RGGLGLS GAKAKYRGGE IRDQNGDSLV HAALVAESAA TGSAEANAFS VLQHVLGAGP HVKRGSNATS SLYQAVAKGV HQP FDVSAF NASYSDSGLF GIYTISQAAS AGDVIKSAYD QVKTIAQGNL SNTDVQAAKN KLKAGYLMSV ESSEGFLDEV GSQA LVAGS YVQPSTVLQQ IDSVADADVI NAAKKFVSGR KSMAASGNLG HTPFVDEL

UniProtKB: Cytochrome b-c1 complex subunit 2, mitochondrial

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Macromolecule #47: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 47 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 42.840715 KDa
SequenceString: MTNIRKSHPL MKIINNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWVIR YLHANGASM FFICLFIHVG RGLYYGSYMF LETWNIGVVL LFTVMATAFM GYVLPWGQMS FWGATVITNL LSAIPYIGTD L VEWIWGGF ...String:
MTNIRKSHPL MKIINNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWVIR YLHANGASM FFICLFIHVG RGLYYGSYMF LETWNIGVVL LFTVMATAFM GYVLPWGQMS FWGATVITNL LSAIPYIGTD L VEWIWGGF SVDKATLTRF FAFHFILPFI ITALAAVHLL FLHETGSNNP TGISSDMDKI PFHPYYTIKD ILGALFMMLI LL ILVLFSP DLLGDPDNYT PANPLNTPPH IKPEWYFLFA YAILRSIPNK LGGVLALVAS ILILILMPML HTSKQRSMMF RPL SQCLFW MLVADLITLT WIGGQPVEHP FIIIGQLASI LYFLIILVLM PITSIIENNL LKW

UniProtKB: Cytochrome b

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Macromolecule #48: Cytochrome c1, heme protein, mitochondrial

MacromoleculeName: Cytochrome c1, heme protein, mitochondrial / type: protein_or_peptide / ID: 48 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 35.35975 KDa
SequenceString: MSAAAAASLR GAVLGPRGAG LPGARARGLL CGPRPGQLPL RTPQALSLSS KSGLSRGRKV ILSALGMLAA GGAGLAVALH SAVSATDLE LHAPSYPWSH RGLLSSLDHT SIRRGFQVYK QVCSSCHSMD YVAYRHLVGV CYTEEEAKAL AEEVEVQDGP N EDGEMFMR ...String:
MSAAAAASLR GAVLGPRGAG LPGARARGLL CGPRPGQLPL RTPQALSLSS KSGLSRGRKV ILSALGMLAA GGAGLAVALH SAVSATDLE LHAPSYPWSH RGLLSSLDHT SIRRGFQVYK QVCSSCHSMD YVAYRHLVGV CYTEEEAKAL AEEVEVQDGP N EDGEMFMR PGKLSDYFPK PYPNPEAARA ANNGALPPDL SYIVRARHGG EDYVFSLLTG YCEPPTGVSL REGLYFNPYF PG QAIAMAP PIYNEVLEFD DGTPATMSQV AKDVCTFLRW ASEPEHDHRK RMGLKMLMMM GLLLPLVYAM KRHKWSVLKS RKL AYRPP

UniProtKB: Cytochrome c1, heme protein, mitochondrial

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Macromolecule #49: Cytochrome b-c1 complex subunit Rieske, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske, mitochondrial / type: protein_or_peptide / ID: 49 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 29.4926 KDa
SequenceString: MLSVASRSGP FAPVLSATSR GVAGALRPLV QAALPATSES PVLDAKRSFL CRESLSGQAA GRPLVASVGL NVPASVRYSH TDIRVPDFS DYRRAEVLDS TKSSKESSDA RKGFSYLITA TTTVGVAYAA KNAVSQFVSS MSASADVLAM SKIEIKLSDI P EGKNMAFK ...String:
MLSVASRSGP FAPVLSATSR GVAGALRPLV QAALPATSES PVLDAKRSFL CRESLSGQAA GRPLVASVGL NVPASVRYSH TDIRVPDFS DYRRAEVLDS TKSSKESSDA RKGFSYLITA TTTVGVAYAA KNAVSQFVSS MSASADVLAM SKIEIKLSDI P EGKNMAFK WRGKPLFVRH RTKKEIDQEA AVEVSQLRDP QHDLERVKKP EWVILIGVCT HLGCVPIANA GDFGGYYCPC HG SHYDASG RIRKGPAPLN LEVPTYEFTS DDLVIVG

UniProtKB: Cytochrome b-c1 complex subunit Rieske, mitochondrial

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Macromolecule #50: Cytochrome b-c1 complex subunit 7

MacromoleculeName: Cytochrome b-c1 complex subunit 7 / type: protein_or_peptide / ID: 50 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 13.587549 KDa
SequenceString:
MASRPAVAAS SKWLEGIRKW YYNAAGFNKL GLMRDDTIYE DDDVKEAIRR LPENLYNDRV FRIKRALDLT MRQQILPKEQ WTKYEEDKF YLEPYLKEVI RERKEREEWA KK

UniProtKB: Cytochrome b-c1 complex subunit 7

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Macromolecule #51: Cytochrome b-c1 complex subunit 8

MacromoleculeName: Cytochrome b-c1 complex subunit 8 / type: protein_or_peptide / ID: 51 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.784339 KDa
SequenceString:
MGREFGHLTR MRHVITYSLS PFEQRAFPHY FTKGIPNVLR RTRACILRVA PPFVVFYLVY TWGTQEFEKS KRKNPAAYEN DK

UniProtKB: Cytochrome b-c1 complex subunit 8

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Macromolecule #52: Cytochrome b-c1 complex subunit 6, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 6, mitochondrial / type: protein_or_peptide / ID: 52 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 10.685803 KDa
SequenceString:
MGLEDEQRML TGSGDPKEEE EEEEELVDPL TTVREQCEQI EKCIKARERL ELCDQRVSSR SQTEEDCTEE LFDFLHARDH CVAHKLFNS LK

UniProtKB: Cytochrome b-c1 complex subunit 6

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Macromolecule #53: Ubiquinol-cytochrome c reductase complex 7.2 kDa protein

MacromoleculeName: Ubiquinol-cytochrome c reductase complex 7.2 kDa protein
type: protein_or_peptide / ID: 53 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 7.41253 KDa
SequenceString:
MAAPTLTARL YSLLFRRTST FALTIAVGAL FFERAFDQGA DAIYEHINQG KLWKHIKHKY ENKE

UniProtKB: Complex III subunit 9

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Macromolecule #54: Cytochrome b-c1 complex subunit 10

MacromoleculeName: Cytochrome b-c1 complex subunit 10 / type: protein_or_peptide / ID: 54 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 6.560654 KDa
SequenceString:
MLSRFLGPRY RELARNWIPT ASMWGAVGAV GLVWATDWRL ILDWVPYING KFKKED

UniProtKB: Cytochrome b-c1 complex subunit 10

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Macromolecule #55: Cytochrome c oxidase subunit 1

MacromoleculeName: Cytochrome c oxidase subunit 1 / type: protein_or_peptide / ID: 55 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 56.992711 KDa
SequenceString: MFVNRWLYST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLLGD DQIYNVIVTA HAFVMIFFMV MPIMIGGFGN WLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSMVE AGAGTGWTVY PPLAGNLAHA GASVDLTIFS LHLAGVSSIL G AINFITTI ...String:
MFVNRWLYST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLLGD DQIYNVIVTA HAFVMIFFMV MPIMIGGFGN WLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSMVE AGAGTGWTVY PPLAGNLAHA GASVDLTIFS LHLAGVSSIL G AINFITTI INMKPPAMSQ YQTPLFVWSV LITAVLLLLS LPVLAAGITM LLTDRNLNTT FFDPAGGGDP ILYQHLFWFF GH PEVYILI LPGFGMISHI VTYYSGKKEP FGYMGMVWAM MSIGFLGFIV WAHHMFTVGM DVDTRAYFTS ATMIIAIPTG VKV FSWLAT LHGGNIKWSP AMLWALGFIF LFTVGGLTGI VLANSSLDIV LHDTYYVVAH FHYVLSMGAV FAIMGGFVHW FPLF SGYTL NQAWAKIHFV IMFVGVNMTF FPQHFLGLSG MPRRYSDYPD AYTAWNTISS MGSFISLTAV MLMIFIIWEA FASKR EVSA VELTSTNLEW LHGCPPPYHT FEEPTYINLK

UniProtKB: Cytochrome c oxidase subunit 1

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Macromolecule #56: Cytochrome c oxidase subunit 2

MacromoleculeName: Cytochrome c oxidase subunit 2 / type: protein_or_peptide / ID: 56 / Number of copies: 1 / Enantiomer: LEVO / EC number: cytochrome-c oxidase
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 26.130471 KDa
SequenceString: (FME)AYPFQLGFQ DATSPIMEEL LHFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE VETIWTILPA IILILI ALP SLRILYMMDE INNPALTVKT MGHQWYWSYE YTDYEDLTFD SYMIPTSDLK PGEMRLLEVD NRVVLPMEMT IRMLVSS ED VLHSWAVPSL ...String:
(FME)AYPFQLGFQ DATSPIMEEL LHFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE VETIWTILPA IILILI ALP SLRILYMMDE INNPALTVKT MGHQWYWSYE YTDYEDLTFD SYMIPTSDLK PGEMRLLEVD NRVVLPMEMT IRMLVSS ED VLHSWAVPSL GLKTDAIPGR LNQTTLMSTR PGLYYGQCSE ICGSNHSFMP IVLELVPLKY FEKWSTSML

UniProtKB: Cytochrome c oxidase subunit 2

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Macromolecule #57: Cytochrome c oxidase subunit 3

MacromoleculeName: Cytochrome c oxidase subunit 3 / type: protein_or_peptide / ID: 57 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 29.753361 KDa
SequenceString: MTHQTHAYHM VNPSPWPLTG ALSALLMTSG LTMWFHFNSM LLLSLGLLTN TLTMYQWWRD IIRESTFQGH HTSVVQKGLR YGMILFIIS EVLFFTGFFW AFYHSSLAPT PELGGCWPPT GIHPLNPLEV PLLNTSILLA SGVSITWAHH SLMEGDRKHM I QALSITIA ...String:
MTHQTHAYHM VNPSPWPLTG ALSALLMTSG LTMWFHFNSM LLLSLGLLTN TLTMYQWWRD IIRESTFQGH HTSVVQKGLR YGMILFIIS EVLFFTGFFW AFYHSSLAPT PELGGCWPPT GIHPLNPLEV PLLNTSILLA SGVSITWAHH SLMEGDRKHM I QALSITIA LGVYFTLLQA SEYYEAPFTI SDGVYGSTFF VATGFHGLHV IIGSTFLAVC LLRQLKFHFT SNHHFGFEAA AW YWHFVDV VWLFLYVSIY WWGS

UniProtKB: Cytochrome c oxidase subunit 3

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Macromolecule #58: Cytochrome c oxidase subunit 4

MacromoleculeName: Cytochrome c oxidase subunit 4 / type: protein_or_peptide / ID: 58 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 19.670664 KDa
SequenceString:
MLATRVFNLI GRRAISTSVC VRAHGSVVKS EDYALPVYVD RRDYPLPDVA HVKNLSASQK ALKEKEKASW SSLSMDEKVE LYRLKFNES FAEMNRSTNE WKTIVGTALF FIGFTALLLI WEKHYVYGPI PHTFEEEWVA KQTKRMLDMK VAPIQGFSAK W DYDKNEWK K

UniProtKB: Cytochrome c oxidase subunit 4

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Macromolecule #59: Cytochrome c oxidase subunit 5A, mitochondrial

MacromoleculeName: Cytochrome c oxidase subunit 5A, mitochondrial / type: protein_or_peptide / ID: 59 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 16.771195 KDa
SequenceString:
MLGAAVRRCS VAAAAVARAS PRGLLHPTPT PGPAAAIQSI RCYSHGSHET DEEFDARWVT YFNKPDIDAW ELRKGMNTLV GYDLVPEPK IIDAALRACR RLNDFASAVR ILEVVKDKAG PHKEIYPYVI QELRPTLNEL GISTPEELGL DKV

UniProtKB: Cytochrome c oxidase polypeptide Va

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Macromolecule #60: Cytochrome c oxidase subunit 5B, mitochondrial

MacromoleculeName: Cytochrome c oxidase subunit 5B, mitochondrial / type: protein_or_peptide / ID: 60 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 13.801783 KDa
SequenceString:
MASRLLRGAG ALAAQTLRAR GPNGVAVVRS MASGGGVPTD EEQATGLERE VMMAARKGLD PYNILAPKAA SGTKEDPNLV PSITNKRIV GCICEEDNST VIWFWVHKGE TQRCPSCGTH YKLVSHQLAH

UniProtKB: Cytochrome c oxidase subunit 5B, mitochondrial

+
Macromolecule #61: Cytochrome c oxidase subunit 6A2

MacromoleculeName: Cytochrome c oxidase subunit 6A2 / type: protein_or_peptide / ID: 61 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 10.87637 KDa
SequenceString:
MALPLRSLSR GLASAAKGDH GGTGARTWRF LTFGLALPSV ALCTLNSWLH SGHHHRPEFI PYHHLRIRTK PYSWGDGNHT LFHNPRVNP LPTGYEQP

UniProtKB: Cytochrome c oxidase subunit

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Macromolecule #62: Cytochrome c oxidase subunit 6B1

MacromoleculeName: Cytochrome c oxidase subunit 6B1 / type: protein_or_peptide / ID: 62 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 10.204456 KDa
SequenceString:
MAEDIQTKIK NYQTAPFDSR FPNQNQTRNC WQNYLDFHRC EKAMTAKGGD VSVCEWYRRV YKSFCPISWV SAWDDRRAEG TFPGKI

UniProtKB: Cytochrome c oxidase subunit

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Macromolecule #63: Cytochrome c oxidase subunit 6C

MacromoleculeName: Cytochrome c oxidase subunit 6C / type: protein_or_peptide / ID: 63 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 8.617122 KDa
SequenceString:
MATSSLTKPQ MRGLLAKRLR FHIVGAFIVS LGVATFYKFA VAEPRKKAYA DFYRNYDSMK DFEEMRKAGI FQSAK

UniProtKB: Cytochrome c oxidase subunit 6C

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Macromolecule #64: Cytochrome c oxidase subunit 7A1, mitochondrial

MacromoleculeName: Cytochrome c oxidase subunit 7A1, mitochondrial / type: protein_or_peptide / ID: 64 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.028479 KDa
SequenceString:
MRALRVSQAL VRSFSSTARN RLENRVAEKQ KIFQADNDLP VHLKGGATDN ILYRVTMTLC LGGTVYSLYC LGWASFPHKK

UniProtKB: Cytochrome c oxidase subunit 7A1, mitochondrial

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Macromolecule #65: Cytochrome c oxidase subunit 7B

MacromoleculeName: Cytochrome c oxidase subunit 7B / type: protein_or_peptide / ID: 65 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.169476 KDa
SequenceString:
MFPLAKNALS RLRVRNIQQT MARQNHQKRA PDFHDKYGNA ILASGATFCV AVWAYTATQI GIEWNLSPVG RVTPKEWREE

UniProtKB: Cytochrome c oxidase subunit 7B, mitochondrial

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Macromolecule #66: Cytochrome c oxidase subunit 7C, mitochondrial

MacromoleculeName: Cytochrome c oxidase subunit 7C, mitochondrial / type: protein_or_peptide / ID: 66 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 7.358661 KDa
SequenceString:
MLGQSIRRFT TSVVRRSHYE EGPGKNLPFS VENKWRLLAM MTLYFGSGFA APFFIVRHQL LKK

UniProtKB: Cytochrome c oxidase subunit 7C, mitochondrial

+
Macromolecule #67: Cytochrome c oxidase subunit 8

MacromoleculeName: Cytochrome c oxidase subunit 8 / type: protein_or_peptide / ID: 67 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 7.615939 KDa
SequenceString:
MLRLAPTVRL LQAPLGGWVV PKAHIYAKPA RTPTSPTEQA IGLSVTFLSF LIPAGWVLSH LDHYKRSSAA

UniProtKB: Cytochrome c oxidase subunit 8

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Macromolecule #68: Cytochrome c oxidase subunit NDUFA4

MacromoleculeName: Cytochrome c oxidase subunit NDUFA4 / type: protein_or_peptide / ID: 68 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.322771 KDa
SequenceString:
MLRQIITQAK KHPSLIPLFV FIGAGGTGAA LYVTRLALFN PDVCWDRKNN PEPWNKLGPN DQYKFFAVNV DYSKLKKEGP DF

UniProtKB: Mitochondrial NDUFA4

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Macromolecule #69: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 69 / Number of copies: 27 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

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Macromolecule #70: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 70 / Number of copies: 15 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM / Phosphatidylcholine

+
Macromolecule #71: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 71 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

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Macromolecule #72: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 72 / Number of copies: 4 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

+
Macromolecule #73: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 73 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

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Macromolecule #74: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 74 / Number of copies: 1 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Macromolecule #75: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 75 / Number of copies: 15 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #76: GUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 76 / Number of copies: 1 / Formula: GTP
Molecular weightTheoretical: 523.18 Da
Chemical component information

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

+
Macromolecule #77: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 77 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #78: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 78 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

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Macromolecule #79: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 79 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #80: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butan...

MacromoleculeName: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate
type: ligand / ID: 80 / Number of copies: 2 / Formula: EHZ
Molecular weightTheoretical: 584.703 Da
Chemical component information

ChemComp-EHZ:
~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate

+
Macromolecule #81: N-ACETYLMETHIONINE

MacromoleculeName: N-ACETYLMETHIONINE / type: ligand / ID: 81 / Number of copies: 1 / Formula: AME
Molecular weightTheoretical: 191.248 Da
Chemical component information

ChemComp-AME:
N-ACETYLMETHIONINE

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Macromolecule #82: MYRISTIC ACID

MacromoleculeName: MYRISTIC ACID / type: ligand / ID: 82 / Number of copies: 1 / Formula: MYR
Molecular weightTheoretical: 228.371 Da
Chemical component information

ChemComp-MYR:
MYRISTIC ACID / Myristic acid

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Macromolecule #83: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 83 / Number of copies: 4 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

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Macromolecule #84: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 84 / Number of copies: 2 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C / Heme C

+
Macromolecule #85: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...

MacromoleculeName: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE
type: ligand / ID: 85 / Number of copies: 15 / Formula: PGV
Molecular weightTheoretical: 749.007 Da
Chemical component information

ChemComp-PGV:
(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / phospholipid*YM / Phosphatidylglycerol

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Macromolecule #86: HEME-A

MacromoleculeName: HEME-A / type: ligand / ID: 86 / Number of copies: 2 / Formula: HEA
Molecular weightTheoretical: 852.837 Da
Chemical component information

ChemComp-HEA:
HEME-A / Heme A

+
Macromolecule #87: COPPER (II) ION

MacromoleculeName: COPPER (II) ION / type: ligand / ID: 87 / Number of copies: 1 / Formula: CU
Molecular weightTheoretical: 63.546 Da
Chemical component information

ChemComp-CU:
COPPER (II) ION / Copper

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Macromolecule #88: SODIUM ION

MacromoleculeName: SODIUM ION / type: ligand / ID: 88 / Number of copies: 1
Molecular weightTheoretical: 22.99 Da

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Macromolecule #89: DINUCLEAR COPPER ION

MacromoleculeName: DINUCLEAR COPPER ION / type: ligand / ID: 89 / Number of copies: 1 / Formula: CUA
Molecular weightTheoretical: 127.092 Da
Chemical component information

ChemComp-CUA:
DINUCLEAR COPPER ION

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Macromolecule #90: (7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)MET...

MacromoleculeName: (7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-17,20-DIEN-1-AMINIUM 4-OXIDE
type: ligand / ID: 90 / Number of copies: 1 / Formula: PSC
Molecular weightTheoretical: 759.068 Da
Chemical component information

ChemComp-PSC:
(7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-17,20-DIEN-1-AMINIUM 4-OXIDE / phospholipid*YM / Phosphatidylcholine

+
Macromolecule #91: (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)...

MacromoleculeName: (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)METHYL]ETHYL (5E,8E,11E,14E)-ICOSA-5,8,11,14-TETRAENOATE
type: ligand / ID: 91 / Number of copies: 2 / Formula: PEK
Molecular weightTheoretical: 768.055 Da
Chemical component information

ChemComp-PEK:
(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)METHYL]ETHYL (5E,8E,11E,14E)-ICOSA-5,8,11,14-TETRAENOATE / phospholipid*YM / Phosphatidylethanolamine

+
Macromolecule #92: PHOSPHATE ION

MacromoleculeName: PHOSPHATE ION / type: ligand / ID: 92 / Number of copies: 1 / Formula: PO4
Molecular weightTheoretical: 94.971 Da
Chemical component information

ChemComp-PO4:
PHOSPHATE ION / Phosphate

+
Macromolecule #93: water

MacromoleculeName: water / type: ligand / ID: 93 / Number of copies: 6327 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER / Water

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.3 µm
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 400000

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