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- EMDB-60319: Respirasome open state 2 in presence of metformin (SC-MetO2) -

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Basic information

Entry
Database: EMDB / ID: EMD-60319
TitleRespirasome open state 2 in presence of metformin (SC-MetO2)
Map data
Sample
  • Complex: Respirasome open state 2 in presence of metformin
    • Protein or peptide: x 67 types
  • Ligand: x 18 types
KeywordsMetformin / electron transport chain / Respirasome / mammalia / MEMBRANE PROTEIN
Function / homology
Function and homology information


Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / Complex IV assembly / Cytoprotection by HMOX1 / TP53 Regulates Metabolic Genes / Complex III assembly / respiratory chain complex IV assembly / Mitochondrial protein import / subthalamus development / pons development ...Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / Complex IV assembly / Cytoprotection by HMOX1 / TP53 Regulates Metabolic Genes / Complex III assembly / respiratory chain complex IV assembly / Mitochondrial protein import / subthalamus development / pons development / : / mitochondrial respirasome assembly / RHOG GTPase cycle / cerebellar Purkinje cell layer development / Complex I biogenesis / : / Respiratory electron transport / pyramidal neuron development / respiratory chain complex IV / thalamus development / Mitochondrial protein degradation / Neutrophil degranulation / mesenchymal stem cell proliferation / respiratory chain complex / reproductive system development / mitochondrial [2Fe-2S] assembly complex / mitochondrial large ribosomal subunit binding / cytochrome-c oxidase / respiratory chain complex III / mesenchymal stem cell differentiation / circulatory system development / oxidative phosphorylation / quinol-cytochrome-c reductase / mitochondrial electron transport, cytochrome c to oxygen / cardiac muscle tissue development / [2Fe-2S] cluster assembly / oxidoreductase activity, acting on NAD(P)H / quinol-cytochrome-c reductase activity / cytochrome-c oxidase activity / stem cell division / mitochondrial electron transport, ubiquinol to cytochrome c / hypothalamus development / midbrain development / acyl binding / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / respiratory chain complex I / response to cAMP / NADH dehydrogenase (ubiquinone) activity / quinone binding / ATP synthesis coupled electron transport / enzyme regulator activity / muscle contraction / reactive oxygen species metabolic process / aerobic respiration / central nervous system development / regulation of mitochondrial membrane potential / respiratory electron transport chain / hippocampus development / DNA damage response, signal transduction by p53 class mediator / kidney development / electron transport chain / fatty acid metabolic process / brain development / metalloendopeptidase activity / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / multicellular organism growth / NAD binding / cellular senescence / FMN binding / nervous system development / 4 iron, 4 sulfur cluster binding / gene expression / oxidoreductase activity / mitochondrial inner membrane / nuclear speck / nuclear body / mitochondrial matrix / copper ion binding / heme binding / structural molecule activity / mitochondrion / proteolysis / nucleoplasm / metal ion binding / membrane
Similarity search - Function
Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Cytochrome c oxidase, subunit 8 / Mitochondrial cytochrome c oxidase subunit VIc/VIIs / Cytochrome c oxidase, subunit 8 superfamily / Mitochondrial cytochrome c oxidase subunit VIc/VIIs superfamily / : / Cytochrome oxidase c subunit VIII / Cytochrome c oxidase subunit VIc ...Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Cytochrome c oxidase, subunit 8 / Mitochondrial cytochrome c oxidase subunit VIc/VIIs / Cytochrome c oxidase, subunit 8 superfamily / Mitochondrial cytochrome c oxidase subunit VIc/VIIs superfamily / : / Cytochrome oxidase c subunit VIII / Cytochrome c oxidase subunit VIc / Cytochrome c oxidase subunit VIIa, metazoa / Cytochrome C oxidase, subunit VIIB / Cytochrome c oxidase subunit IV / Cytochrome C oxidase, subunit VIIB domain superfamily / Cytochrome c oxidase, subunit VIIa superfamily / Cytochrome C oxidase chain VIIB / Cytochrome c oxidase, subunit VIa, conserved site / Cytochrome c oxidase subunit VIa signature. / Cytochrome c oxidase, subunit VIa / Cytochrome c oxidase, subunit VIa superfamily / Cytochrome c oxidase subunit VIa / Cytochrome c oxidase, subunit VIb / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / : / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Cytochrome c oxidase subunit Vb, zinc binding region signature. / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV family / Cytochrome c oxidase, subunit VIb superfamily / 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 2, C-terminal / Cytochrome oxidase c subunit VIb / Cytochrome c oxidase, subunit Va/VI / Cytochrome c oxidase, subunit Va/VI superfamily / Cytochrome c oxidase subunit Va / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit VII / Globular protein, non-globular alpha/beta subunit / Cytochrome c oxidase, subunit Vb / Cytochrome c oxidase subunit III domain / Cytochrome c oxidase subunit Vb / Cytochrome c oxidase subunit Vb, zinc binding domain profile. / Cytochrome c oxidase, subunit II / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome c oxidase subunit I domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome b-c1 complex, subunit 6 / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / 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 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 9 superfamily / Cytochrome c/quinol oxidase subunit II / Cytochrome b-c1 complex subunit 9 / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / : / Cytochrome b / Cytochrome C oxidase subunit II, transmembrane domain superfamily / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / 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 dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH:ubiquinone oxidoreductase, ESSS subunit / ESSS subunit of NADH:ubiquinone oxidoreductase (complex I) / : / Cytochrome c oxidase subunit I / Cytochrome b/b6, C-terminal / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome b(C-terminal)/b6/petD / Cytochrome C and Quinol oxidase polypeptide I / Cytochrome b/b6 C-terminal region profile. / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Cytochrome C oxidase subunit II, periplasmic domain / Cytochrome b/b6, C-terminal domain superfamily
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / Acyl carrier protein / Cytochrome c oxidase subunit / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / Cytochrome c oxidase subunit 7B, mitochondrial / NADH dehydrogenase [ubiquinone] 1 subunit C2 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial ...NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / Acyl carrier protein / Cytochrome c oxidase subunit / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / Cytochrome c oxidase subunit 7B, mitochondrial / NADH dehydrogenase [ubiquinone] 1 subunit C2 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / 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 dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / Cytochrome c oxidase subunit / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome c oxidase subunit 6C / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 8 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 / Cytochrome b-c1 complex subunit 10 / Cytochrome c oxidase subunit 8 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial / : / Cytochrome b-c1 complex subunit 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / Cytochrome b-c1 complex subunit 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Cytochrome b-c1 complex subunit 6 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / Cytochrome c oxidase subunit 5A, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 2 / Cytochrome c oxidase subunit 1 / NADH-ubiquinone oxidoreductase chain 3 / NADH-ubiquinone oxidoreductase chain 6 / Cytochrome c oxidase subunit 2 / NADH-ubiquinone oxidoreductase chain 4L / Cytochrome b / Cytochrome c oxidase subunit 7C, mitochondrial / Complex III subunit 9 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 / Cytochrome c oxidase subunit 3 / Cytochrome c oxidase subunit 5B, mitochondrial / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 4 / Cytochrome c oxidase subunit 7A1, mitochondrial
Similarity search - Component
Biological speciesSus scrofa (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.01 Å
AuthorsTeng F / He ZX / Hu YQ / Xu CY / Guo RY / Zhou L
Funding support China, 1 items
OrganizationGrant numberCountry
Other governmentZJU100 Young Professor China
CitationJournal: Nat Struct Mol Biol / Year: 2025
Title: Hydrophilic metformin and hydrophobic biguanides inhibit mitochondrial complex I by distinct mechanisms.
Authors: Zhaoxiang He / Fei Teng / Yanqing Yang / Ruiyang Guo / Mengchen Wu / Fangzhu Han / Hongtao Tian / Jiawei Wang / Yiqi Hu / Yangwei Jiang / Leili Zhang / Chenyang Xu / Fan Yang / Jiancang Zhou ...Authors: Zhaoxiang He / Fei Teng / Yanqing Yang / Ruiyang Guo / Mengchen Wu / Fangzhu Han / Hongtao Tian / Jiawei Wang / Yiqi Hu / Yangwei Jiang / Leili Zhang / Chenyang Xu / Fan Yang / Jiancang Zhou / Shan Zhang / James A Letts / Ruhong Zhou / Long Zhou /
Abstract: Metformin is the only antihyperglycemic biguanide targeting type 2 diabetes mellitus with proven safety. Although a mechanism of action involving tight inhibition of the respiratory complex I has ...Metformin is the only antihyperglycemic biguanide targeting type 2 diabetes mellitus with proven safety. Although a mechanism of action involving tight inhibition of the respiratory complex I has been proposed for hydrophobic biguanides, it remains elusive for the hydrophilic metformin, whose excellent pharmacological tolerance depends on weak complex I inhibition without competitive nature. Here we solved cryo-electron microscopy structures of the metformin-bound porcine respirasome. Our structural and kinetic data are consistent with a model in which metformin enters complex I only in its open state and becomes trapped at the ubiquinone redox site by ubiquinone-induced conformational closing of the enzyme. By contrast, the hydrophobic proguanil alone occupies both the entrance and the redox site of the ubiquinone channel in open and closed complex I and is kinetically consistent with competitive inhibition with conformation-dependent affinities. Our data provide the molecular basis for metformin's well-known superior properties, such as a wide therapeutic window and positive ubiquinone cooperativity, leading to its clinical success and facilitating future therapeutic developments.
History
DepositionMay 29, 2024-
Header (metadata) releaseNov 19, 2025-
Map releaseNov 19, 2025-
UpdateNov 19, 2025-
Current statusNov 19, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_60319.png

Downloads & links

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Map

FileDownload / File: emd_60319.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
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AxesX (Sec.)Y (Row.)Z (Col.)
1.2 Å/pix.
x 480 pix.
= 576. Å		1.2 Å/pix.
x 480 pix.
= 576. Å		1.2 Å/pix.
x 480 pix.
= 576. Å

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Voxel sizeX=Y=Z: 1.2 Å
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Contour LevelBy AUTHOR: 6.0
Minimum - Maximum-24.261092999999999 - 47.82076
Average (Standard dev.)-0.003155788 (±1.0782585)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 576.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_60319_msk_1.map
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Half map: #2

Fileemd_60319_half_map_1.map
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Half map: #1

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Sample components

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Entire : Respirasome open state 2 in presence of metformin

EntireName: Respirasome open state 2 in presence of metformin
Components
  • Complex: Respirasome open state 2 in presence of metformin
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4L
    • 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
    • Protein or peptide: Cytochrome c oxidase subunit
    • 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, mitochondrial
    • Protein or peptide: Cytochrome c oxidase subunit 7C, mitochondrial
    • Protein or peptide: Cytochrome c oxidase subunit 8
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
    • Protein or peptide: Complex I-B14.5a
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
    • Protein or peptide: Acyl carrier protein
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
    • Protein or peptide: Complex I-B17
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
    • 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 beta subcomplex subunit 11, mitochondrial
    • 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: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 subunit C2
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 1
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 2
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 3
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 4
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 5
    • Protein or peptide: NADH-ubiquinone oxidoreductase chain 6
    • Protein or peptide: Cytochrome b-c1 complex subunit 2, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 1, mitochondrial
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome c domain-containing protein
    • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 6
    • Protein or peptide: Cytochrome b-c1 complex subunit 7
    • Protein or peptide: Cytochrome b-c1 complex subunit 8
    • Protein or peptide: Complex III subunit 9
    • Protein or peptide: Cytochrome b-c1 complex subunit 10
    • Protein or peptide: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    • Protein or peptide: Complex I-49kD
    • Protein or peptide: Complex I-30kD
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
    • Protein or peptide: Complex I-9kD
  • Ligand: CARDIOLIPIN
  • Ligand: ZINC ION
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL
  • Ligand: HEME-A
  • Ligand: COPPER (II) ION
  • Ligand: MAGNESIUM ION
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: HEME C
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE
  • Ligand: IRON/SULFUR CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE

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Supramolecule #1: Respirasome open state 2 in presence of metformin

SupramoleculeName: Respirasome open state 2 in presence of metformin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#67
Source (natural)Organism: Sus scrofa (pig)

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Macromolecule #1: NADH-ubiquinone oxidoreductase chain 4L

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4L / 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: 10.827253 KDa
SequenceString:
MPLVYMNIIM AFAIALAGLL MYRSHLMSSL LCLEGMMLSL FIMSTLIILN THFTLANMMP IILLVFAACE AALGLSLLVM VSNTYGTDY VQNLNLLQC

UniProtKB: NADH-ubiquinone oxidoreductase chain 4L

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Macromolecule #2: Cytochrome c oxidase subunit 5A, mitochondrial

MacromoleculeName: Cytochrome c oxidase subunit 5A, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 11.717335 KDa
SequenceString:
TDEEFDARWV TYFNKPDIDA WELRKGMNTL VGYDLVPEPK IIDAALRACR RLNDFASAVR ILEVVKDKAG PHKEIYPYVI QELRPTLNE LGISTPEELG LDK

UniProtKB: Cytochrome c oxidase subunit 5A, mitochondrial

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Macromolecule #3: Cytochrome c oxidase subunit 5B, mitochondrial

MacromoleculeName: Cytochrome c oxidase subunit 5B, mitochondrial / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 10.382739 KDa
SequenceString:
SGGGVPTDEE QATGLEREVM MAARKGLDPY NILAPKAASG TKEDPNLVPS ITNKRIVGCI CEEDNSTVIW FWVHKGETQR CPSCGTHYK LVSHQL

UniProtKB: Cytochrome c oxidase subunit 5B, mitochondrial

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Macromolecule #4: Cytochrome c oxidase subunit

MacromoleculeName: Cytochrome c oxidase subunit / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 8.724874 KDa
SequenceString:
TGARTWRFLT FGLALPSVAL CTLNSWLHSG HHHRPEFIPY HHLRIRTKPY SWGDGNHTLF HNPRVNPLPT GYEQP

UniProtKB: Cytochrome c oxidase subunit

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Macromolecule #5: Cytochrome c oxidase subunit

MacromoleculeName: Cytochrome c oxidase subunit / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.723963 KDa
SequenceString:
IQTKIKNYQT APFDSRFPNQ NQTRNCWQNY LDFHRCEKAM TAKGGDVSVC EWYRRVYKSL CPISWVSAWD DRRAEGTFPG KI

UniProtKB: Cytochrome c oxidase subunit

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Macromolecule #6: Cytochrome c oxidase subunit 6C

MacromoleculeName: Cytochrome c oxidase subunit 6C / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 8.139589 KDa
SequenceString:
LTKPQMRGLL AKRLRFHIVG AFIVSLGVAT FYKFAVAEPR KKAYADFYRN YDSMKDFEEM RKAGIFQSAK

UniProtKB: Cytochrome c oxidase subunit 6C

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

MacromoleculeName: Cytochrome c oxidase subunit 7A1, mitochondrial / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 6.376324 KDa
SequenceString:
LENRVAEKQK IFQADNDLPV HLKGGATDNI LYRVTMTLCL GGTVYSLYCL GWASFPH

UniProtKB: Cytochrome c oxidase subunit 7A1, mitochondrial

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Macromolecule #8: Cytochrome c oxidase subunit 7B, mitochondrial

MacromoleculeName: Cytochrome c oxidase subunit 7B, mitochondrial / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 5.543207 KDa
SequenceString:
APDFHDKYGN AILASGATFC VAVWAYTATQ IGIEWNLSPV GRVTPKEWRE

UniProtKB: Cytochrome c oxidase subunit 7B, mitochondrial

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Macromolecule #9: Cytochrome c oxidase subunit 7C, mitochondrial

MacromoleculeName: Cytochrome c oxidase subunit 7C, mitochondrial / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 5.465396 KDa
SequenceString:
SHYEEGPGKN LPFSVENKWR LLAMMTLYFG SGFAAPFFIV RHQLLKK

UniProtKB: Cytochrome c oxidase subunit 7C, mitochondrial

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Macromolecule #10: Cytochrome c oxidase subunit 8

MacromoleculeName: Cytochrome c oxidase subunit 8 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 4.776493 KDa
SequenceString:
IYAKPARTPT SPTEQAIGLS VTFLSFLIPA GWVLSHLDHY KRS

UniProtKB: Cytochrome c oxidase subunit 8

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
type: protein_or_peptide / ID: 11 / 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 #12: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.770203 KDa
SequenceString:
LGLREIRIHL CQRSPGSQGV RDFIEKRYVE LKKANPDLPI LIRECSDVQP KLWARYAFGQ EKNVSLNNFS ADQVTRTLEN VLSGK

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

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Macromolecule #13: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.094372 KDa
SequenceString:
AGRIASFLKN AWAKEPVLVA SFAIGGLAII LPSLSPYTNY AIRINRATPY NYPVPLRDDG NMPDVPSHPQ DPQGPSLEWL KNL

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

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Macromolecule #14: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.949106 KDa
SequenceString:
LKKTTGLVGL AVCETPHERL KILYTKILDV LGQIPKNAAY RKYTEQITNE KLGMVKAEPD VKKLEEQLQG GQIEEVILQA ENELSLARK MLRWKPWEPL VEEPPANQWK WPI

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

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Macromolecule #15: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 13.755924 KDa
SequenceString:
TSVKPIFSRD MNEAKRRVRE LYRAWYREVP NTVHLFQLDI SVKQGRDKVR EMFMKNAHVT DPRVVDLLVI KGKMELEETI NVWKQRTHI MRFFHETEAP RPTDFLSKFY VGHDP

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

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Macromolecule #16: Complex I-B14.5a

MacromoleculeName: Complex I-B14.5a / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.517394 KDa
SequenceString:
ASATRVIQLL RNWASGRDLQ AKLQLRYQEI SKRTQPPPKL PVGPSHKLSN NYYCTRDGRR EAMPPSIVMS SQKVLASGKP AESSAVAET EKKAVTPAPP IKRWELSKDQ PYL

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

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Macromolecule #17: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 19.932898 KDa
SequenceString:
PGIVELPTLE DLKVQEVKVS SSVLKAAAHH YGAQCDKPNK EFMLCRWEEK DPRRCLEEGK LVNQCALDFF RQIKRHCAEP FTEYWTCID YSGLQLFRHC RKQQAKFDEC VLDKLGWVRP DLGELSKVTK VKTDRPLPEN PYHSRARPEP NPEAEGDLKP A KHGSRLFF WTM

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

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Macromolecule #18: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 38.840895 KDa
SequenceString: LHHALIPHGK GGRSSVSGIV ATVFGATGFL GRYVVNHLGR MGSQVIVPYR CEPYDTMHLR PMGDLGQIIF MEWNGKDKDS IRKVVEHSN VVINLVGREW ETKNFDFEDV FVKIPHAIAQ VSKEAGVEKL IHISHLNADI KSPSRYLRSK AVGEKEVRAA F PEATIIKP ...String:
LHHALIPHGK GGRSSVSGIV ATVFGATGFL GRYVVNHLGR MGSQVIVPYR CEPYDTMHLR PMGDLGQIIF MEWNGKDKDS IRKVVEHSN VVINLVGREW ETKNFDFEDV FVKIPHAIAQ VSKEAGVEKL IHISHLNADI KSPSRYLRSK AVGEKEVRAA F PEATIIKP SDIFGREDRF LNYFASMRWF GGVPLISLGK ETVKQPVYIV DVSKGIINAI KDPDAKGKTF AFVGPNRYLL FD LVQYIFA VAYRPFLPYP LPHFAYRWVG RLFEVSPFEP WTTRDKVERV HMSDMTLPHL PGLEDLGIQA TPLELKAIEV LRR HRTYRW LTSEMEDVKP AKTVN

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

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Macromolecule #19: Acyl carrier protein

MacromoleculeName: Acyl carrier protein / type: protein_or_peptide / ID: 19 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 17.308186 KDa
SequenceString:
MAARVLCACV RRLPAAFAPL PRIPTVVAAR PLSTTLFPTG AQARSRALQP ALVLAQAPGG VTQLCRRYSD APPLTLEAIK DRVLYVLKL YDKIDPEKLS VNSHFMKDLG LDSLDQVEII MAMEDEFGFE IPDIDAEKLM CPQEIVDYIA DKKDVYE

UniProtKB: Acyl carrier protein

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Macromolecule #20: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mi...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 36.79268 KDa
SequenceString: LQYGPLAFVL GERTTRKLTE TSKVITVDGN ICSGKGRLAR EIAEKLGLRH FPEAGIHYAD STTGDGKPLD VQLSGNCSLE KFYDDPKSN DGNSYRLQSW LYASRLLQYA DALEHLLSTG QGVVLERSIY SDFVFLEAMY RQGFIRKQCV EHYNEVKKVT A CEYLPPHV ...String:
LQYGPLAFVL GERTTRKLTE TSKVITVDGN ICSGKGRLAR EIAEKLGLRH FPEAGIHYAD STTGDGKPLD VQLSGNCSLE KFYDDPKSN DGNSYRLQSW LYASRLLQYA DALEHLLSTG QGVVLERSIY SDFVFLEAMY RQGFIRKQCV EHYNEVKKVT A CEYLPPHV VVYVDVPVPE IQSRIQKKGN PHEMKITAAY LQDIENAYKK TFLPEMSEKC EVLQYSAREA EDAEKVVEDI EY LKCDKGP WPDQDDRTFH RLRMLVQNKL EVLNYTTIPV YLPEITIGAH QSDRVFQKFT ELPGRKYSPG YNEDVGDKWI WLK

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

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Macromolecule #21: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.555698 KDa
SequenceString:
AKTLLHKYSD IPEGTECHRK AYASTSIGGA TGLIVSAYSI ALKPPASFLE GVARTGRYTF TSAAIGAIFG LTSCISAQVR EKPDDPLNY FIGGCAGGLT LGARTRSYGI GAAACAYMGL TAALVKMGQL EGWQVFAEPK V

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

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Macromolecule #22: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 17.031244 KDa
SequenceString:
ELVQVLRRGL QQVSGHGGLR GYLRVLFRAN DVRVGTLVGE DKYGNKYYED NKQFFGRHRW VIYTTEMNGR DTFWDVDGSM VPPEWHRWL HCMTDDPPTT KPPTARKYIW TNHKFNVSGT PQQYVPYSTT RKKIQEWVPP STPYK

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

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Macromolecule #23: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 16.70934 KDa
SequenceString:
ASKVKQDMPP PGGYGPIDYK RNLPRRGLSG YSMFAVGIGT LLFGYWSMMK WNRERRRLQI EDFEARIALM PLFQAEKDRR VLQMLRENL EEEAIIMKDV PDWKVGESVF HTTRWVTPMM GELYGLRTNE EILSATYGFI WYT

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

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 6.781886 KDa
SequenceString:
NVLQIVRDHW VHILVPVGFV FGCYLDRRSD EKLTAFRNKS LLFKRELRPN EEVTWK

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

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Macromolecule #25: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial
type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 8.201093 KDa
SequenceString:
VHIEPRYRQF PQLTRSQLIQ AEFFSATMWF WILWRFWHDS DAVLGHFPYP DPSQWTDEEL GILPDDE

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

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Macromolecule #26: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.042212 KDa
SequenceString:
SKMELPDYKQ WKIEGTPLET VQEKLAARGL RDPWGRNEAW RYSGGFANNV SFVGALLKGF KWGFAAFVVA VGAEYYLESQ

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

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Macromolecule #27: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.986153 KDa
SequenceString:
SFPKYKPSRL ATLPATLDPA EYDISPETRK AQAERLAIRS RLKREYLLQY NDPNRLGVIE DPALIRWTYA RSANIYPNFR PTPKTSLLG ALFGIGPLFF WYYVFKTDRD KKEKLIQEGK LDQTFNISY

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

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Macromolecule #28: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
type: protein_or_peptide / ID: 28 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 16.281898 KDa
SequenceString:
KRLFIIKPSG FYDRRFLKLM RFYILLTGIP VAIGITLVNV FIGEAELADI PEGYVPEHWE YFKHPISRWI ARTFYDGPEK NYEKTMAIL QIEAEKAELR LKELEVRRLM RARGDGPWYQ YPTIDKALID HSPKTTPDN

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

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Macromolecule #29: Complex I-B17

MacromoleculeName: Complex I-B17 / type: protein_or_peptide / ID: 29 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 15.333832 KDa
SequenceString:
SGYTPDEKLR LQQLRELRRR WLKDQELSPR EPVLPPRRVW PMEQFWNKFL QDGAPWKNVI YKTYRHSIFA VTHVLIPVWI IHYYLKYHV TAKPYTVVER KPRIFPGDTI LETGEVIPLM KEFPDQH

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

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Macromolecule #30: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
type: protein_or_peptide / ID: 30 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 15.307553 KDa
SequenceString:
MGAHLARRYL GDASKEPDPL RMPTFPPDYG FPERKEREMV ATQQEMNDAQ LMLQQRDYCA HYLIQLLKCK RDSFPNFLAC KHEQHDWDY CEHLDYVKRM KEFERERRLL QRKKRREQRE AEMARG

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

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Macromolecule #31: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 18.608805 KDa
SequenceString:
HVTKDMFPGP YPKTPEERAA AAKKYNMRVE DYEPYPDDGM GYGDYPKLPD RSQQERDPWY DWDHPDLRLN WGEPIHWDLD MYIRNRVDT SPTPVSWNTM CKHLFGFVAF MLFMFWVGEI YPSYQPVGPK QYPYNDLYLE RGGDPTKEPE PVVHYEI

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

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Macromolecule #32: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
type: protein_or_peptide / ID: 32 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 21.733711 KDa
SequenceString:
AFSAPAAYLT HQQKVLRLYK RALRHLESWC VHRDKYRYFA CLMRARFDEH KNEKDMVKAT QLLRQAEEEF WYGQHPQPYI FPESPGGTS YERYECYKVP EWCLDDWHPS EKAMYPDYFA KREQWKRLRR ESWEREVKQL QEETPPGGPR TEALPPARKE G DLPPLWWH IVTRPRERPM

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

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Macromolecule #33: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
type: protein_or_peptide / ID: 33 / 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 #34: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial
type: protein_or_peptide / ID: 34 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.113493 KDa
SequenceString:
IRLQEDPDPE DENLYEKNPD SHGYDKDPIV DLWNMRVVFF FGFSIVLVLG STFVAYLPDY RMQEWARREA ERLVKYREAN GLPLMESNC FDPNKIQLPE DED

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

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Macromolecule #35: Cytochrome c oxidase subunit 1

MacromoleculeName: Cytochrome c oxidase subunit 1 / type: protein_or_peptide / ID: 35 / Number of copies: 1 / Enantiomer: LEVO / EC number: cytochrome-c oxidase
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 #36: Cytochrome c oxidase subunit 2

MacromoleculeName: Cytochrome c oxidase subunit 2 / type: protein_or_peptide / ID: 36 / Number of copies: 1 / Enantiomer: LEVO / EC number: cytochrome-c oxidase
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 26.203564 KDa
SequenceString: MAYPFQLGFQ DATSPIMEEL LHFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE VETIWTILPA IILILIALPS LRILYMMDE INNPALTVKT MGHQWYWSYE YTDYEDLTFD SYMIPTSDLK PGEMRLLEVD NRVVLPMEMT IRMLVSSEDV L HSWAVPSL ...String:
MAYPFQLGFQ DATSPIMEEL LHFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE VETIWTILPA IILILIALPS LRILYMMDE INNPALTVKT MGHQWYWSYE YTDYEDLTFD SYMIPTSDLK PGEMRLLEVD NRVVLPMEMT IRMLVSSEDV L HSWAVPSL GLKTDAIPGR LNQTTLMSTR PGLYYGQCSE ICGSNHSFMP IVLELVPLKY FEKWSTSMLT

UniProtKB: Cytochrome c oxidase subunit 2

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Macromolecule #37: Cytochrome c oxidase subunit 3

MacromoleculeName: Cytochrome c oxidase subunit 3 / type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO / EC number: cytochrome-c oxidase
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 #38: Cytochrome c oxidase subunit 4

MacromoleculeName: Cytochrome c oxidase subunit 4 / type: protein_or_peptide / ID: 38 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 16.323619 KDa
SequenceString:
EDYALPVYVD RRDYPLPDVA HVKNLSASQK ALKEKEKASW SSLSMDEKVE LYRLKFNESF AEMNRSTNEW KTIVGTALFF IGFTALLLI WEKHYVYGPI PHTFEEEWVA KQTKRMLDMK VAPIQGFSAK WDYDKNEWK

UniProtKB: Cytochrome c oxidase subunit 4

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Macromolecule #39: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
type: protein_or_peptide / ID: 39 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 5.881825 KDa
SequenceString:
KFYIREPPHG SPDWLKVGLT LGTSVFLWIY LIKQHKEDVL EYKRRNGLE

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

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Macromolecule #40: NADH dehydrogenase [ubiquinone] 1 subunit C2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 subunit C2 / type: protein_or_peptide / ID: 40 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.196459 KDa
SequenceString:
TMMSGRPGRV PLQFLPNEAR SLPPPKLTDP RLVYMGFLGY CSGLIDNAIR RRPVVSAGLH RQLLYVTSFV FFGYYLLKRQ DYMYALRDH DMFAYVKSHP EDFPEKDKKT YGEILEEFHP VR

UniProtKB: NADH dehydrogenase [ubiquinone] 1 subunit C2

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Macromolecule #41: NADH-ubiquinone oxidoreductase chain 1

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 1 / type: protein_or_peptide / ID: 41 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 35.66752 KDa
SequenceString: MFMINILSLI IPILLAVAFL TLVERKVLGY MQLRKGPNVV GPYGLLQPIA DALKLFTKEP LRPATSSISM FIIAPILALS LALTMWVPL PMPYPLINMN LGVLFMLAMS SLAVYSILWS GWASNSKYAL IGALRAVAQT ISYEVTLAII LLSVLLMNGS Y TLSTLITT ...String:
MFMINILSLI IPILLAVAFL TLVERKVLGY MQLRKGPNVV GPYGLLQPIA DALKLFTKEP LRPATSSISM FIIAPILALS LALTMWVPL PMPYPLINMN LGVLFMLAMS SLAVYSILWS GWASNSKYAL IGALRAVAQT ISYEVTLAII LLSVLLMNGS Y TLSTLITT QEHIWMIFTS WPLAMMWFIS TLAETNRAPF DLTEGESELV SGFNVEYAAG PFAMFFMAEY ANIIMMNAFT AI LFLGASH DPHTPELYTI NFVLKTLALT ITFLWIRASY PRFRYDQLMH LLWKSFLPLT LALCMWHISL PIMTASIPPQ S

UniProtKB: NADH-ubiquinone oxidoreductase chain 1

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Macromolecule #42: NADH-ubiquinone oxidoreductase chain 2

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 2 / type: protein_or_peptide / ID: 42 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 39.077504 KDa
SequenceString: MNPIIYTTLI MTVMSGTMLV MISSHWLLIW IGFEMNLLAM IPVLMKNFNP RATEAATKYF LTQATASMML MMAIIINLLY SGQWTITKM FNPVAMTMMT MALAMKLGLS PFHFWVPEVT QGISLQAGLL LLTWQKLAPL SVLCQISQSI NPNLMLTMAM L SILIGGWG ...String:
MNPIIYTTLI MTVMSGTMLV MISSHWLLIW IGFEMNLLAM IPVLMKNFNP RATEAATKYF LTQATASMML MMAIIINLLY SGQWTITKM FNPVAMTMMT MALAMKLGLS PFHFWVPEVT QGISLQAGLL LLTWQKLAPL SVLCQISQSI NPNLMLTMAM L SILIGGWG GLNQTQLRKI MAYSSIAHMG WMTAVLPYNT TMTILNLLIY ITMTLAMFML LIHSSATTTL SLSHTWNKMP VI TSLMMVT LLSMGGLPPL SGFMPKWMII QEMTKNESII MPTLMAMTAL LNLYFYMRLA YSSSLTMFPS TNNMKMKWQF EHT KQMKLL PTMIVLSTLV LPMTPALSSL N

UniProtKB: NADH-ubiquinone oxidoreductase chain 2

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Macromolecule #43: NADH-ubiquinone oxidoreductase chain 3

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 3 / type: protein_or_peptide / ID: 43 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.869334 KDa
SequenceString:
MNIMLTLLTN VTLASLLVLI AFWLPQLNAY SEKTSPYECG FDPMGSARLP FSMKFFLVAI TFLLFDLEIA LLLPLPWASQ TNNLKTMLT MALFLLILLA ASLAYEWTQK GLEWA

UniProtKB: NADH-ubiquinone oxidoreductase chain 3

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Macromolecule #44: NADH-ubiquinone oxidoreductase chain 4

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 4 / type: protein_or_peptide / ID: 44 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 51.853355 KDa
SequenceString: MLKIIIPTTM LLPMTWMSKH NMIWINATVH SLLISLISLS LLNQLGENSL NFSLTFFSDS LSAPLLVLTT WLLPLMLMAS QSHLSKETT TRKKLYITML ILLQLFLIMT FTATELILFY ILFEATLVPT LIIITRWGNQ TERLNAGLYF LFYTLAGSLP L LVALVYIQ ...String:
MLKIIIPTTM LLPMTWMSKH NMIWINATVH SLLISLISLS LLNQLGENSL NFSLTFFSDS LSAPLLVLTT WLLPLMLMAS QSHLSKETT TRKKLYITML ILLQLFLIMT FTATELILFY ILFEATLVPT LIIITRWGNQ TERLNAGLYF LFYTLAGSLP L LVALVYIQ NTTGSLNFLI IHYWSHPLSN SWSNIFMWLA CIMAFMVKMP LYGLHLWLPK AHVEAPIAGS MVLAAVLLKL GG YGMMRIT TILNPLTNYM AYPFLMLSMW GMIMTSSICL RQTDLKSLIA YSSVSHMALV IVAIMIQTPW SFMGATALMI AHG LTSSML FCLANTNYER VHSRTMILAR GLQTLLPLMA TWWLVASLTN LALPPSINLI GELFIITASF SWSNITIILM GMNM MITAL YSLYMLITTQ RGKYTHHINN IKPSFTRENA LMALHILPLL LLTLNPKMIL GPLY

UniProtKB: NADH-ubiquinone oxidoreductase chain 4

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Macromolecule #45: NADH-ubiquinone oxidoreductase chain 5

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 5 / type: protein_or_peptide / ID: 45 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 68.267031 KDa
SequenceString: MNPFASLTLT TLTILTIPIM MSNSNIYKTN LYPNYVKTTV SYAFTLSLVP LLMFMHTGQE MIISNWHWMT LQTVELSLSF KMDYFSVMF IPVALFVTWS IMEFSMWYMH SDPFINRFFK YLLLFLITMM ILVTANNLFQ LFIGWEGVGI MSFLLIGWWH G RTDANTAA ...String:
MNPFASLTLT TLTILTIPIM MSNSNIYKTN LYPNYVKTTV SYAFTLSLVP LLMFMHTGQE MIISNWHWMT LQTVELSLSF KMDYFSVMF IPVALFVTWS IMEFSMWYMH SDPFINRFFK YLLLFLITMM ILVTANNLFQ LFIGWEGVGI MSFLLIGWWH G RTDANTAA LQAILYNRIG DIGFVLSMAW FLTHSNAWDL QQIFMLNNEC PNMPLIGLLL AAAGKSAQFG LHPWLPSAME GP TPVSALL HSSTMVVAGV FLLIRFYPLM ETNKLVQTMT LCLGAITTLF TALCAITQND IKKIVAFSTS SQLGLMMVTI GIN QPHLAF LHICMHAFFK AMLFMCSGSI IHSLNDEQDI RKMGGLYKAM PFTTTALIIG SLALTGMPYL TGFYSKDLII EAVN MSYTN AWALLMTLIA TSLTAAYSTR IIFFAFLGKP RFPPLVLINE NNPLLINSIK RLLIGSIFAG FIISNNIPPM TVPNT TMPL YMKMTALIVT IMGFMLALEL NNTTYYLKFK YPSQTYKFSN MLGYYPSIMH RLPTYHNLSM SQKSASSLLD LIWLET ILP KTTSFIQMKM SIMVSNQKGL IKLYFLSFLI TIMISMTLFN

UniProtKB: NADH-ubiquinone oxidoreductase chain 5

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Macromolecule #46: NADH-ubiquinone oxidoreductase chain 6

MacromoleculeName: NADH-ubiquinone oxidoreductase chain 6 / type: protein_or_peptide / ID: 46 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 18.890135 KDa
SequenceString:
TMYIAFILST IFVIGFVGFS SKPSPIYGGL GLIVSGGVGC GIVLNFGGSF LGLMVFLIYL GGMLVVFGYT TAMATEMYPE VWVSNKTVF GAFVSGLMME FCMVYYALKE EEVEIIFKFN GLGDWVIYDT GDSGFFSEEA MGIAALYSYG TWLVIVTGWS L LIGVVVIM EITRGN

UniProtKB: NADH-ubiquinone oxidoreductase chain 6

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Macromolecule #47: Cytochrome b-c1 complex subunit 2, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 2, mitochondrial / type: protein_or_peptide / ID: 47 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 44.727215 KDa
SequenceString: PQDLEFTRLP NGLVIASLEN YAPASRIGLF IKAGSRYEDS NNLGTSHLLR LASSLTTKGA SSFKITRGIE AVGGKLSVTS TRESMAYTV ECLRDDIEIL MEFLLNVTAA PEFRRWEVAA LQSQLRIDKA VAFQNPQAQV LENLHAAAYR NALANSLYCP D YRIGKVTP ...String:
PQDLEFTRLP NGLVIASLEN YAPASRIGLF IKAGSRYEDS NNLGTSHLLR LASSLTTKGA SSFKITRGIE AVGGKLSVTS TRESMAYTV ECLRDDIEIL MEFLLNVTAA PEFRRWEVAA LQSQLRIDKA VAFQNPQAQV LENLHAAAYR NALANSLYCP D YRIGKVTP DQLHYYVQNH FTSARMALIG LGVSHPVLKQ VAERFLNMRG GLGLSGAKAK YRGGEIRDQN GDSLVHAALV AE SAATGSA EANAFSVLQH VLGAGPHVKR GSNATSSLYQ AVAKGVHQPF DVSAFNASYS DSGLFGIYTI SQAASAGDVI KSA YDQVKT IAQGNLSNTD VQAAKNKLKA GYLMSVESSE GFLDEVGSQA LVAGSYVQPS TVLQQIDSVA DADVINAAKK FVSG RKSMA ASGNLGHTPF VDEL

UniProtKB: Cytochrome b-c1 complex subunit 2, mitochondrial

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Macromolecule #48: Cytochrome b-c1 complex subunit 1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 1, mitochondrial / type: protein_or_peptide / ID: 48 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 49.270133 KDa
SequenceString: TATYAQALQS VPETQVSQLD NGLRVASEQS SQPTCTVGVW IDAGSRYENE KNNGAGYFVE HLAFKGTKNR PGSALEKEVE SMGAHLNAY STREHTAYYI KALSKDLPKA VELLADIVQN CSLEDSQIEK ERDVILQELQ ENDSSMRDVV FDYLHATAFQ G TPLAQSVE ...String:
TATYAQALQS VPETQVSQLD NGLRVASEQS SQPTCTVGVW IDAGSRYENE KNNGAGYFVE HLAFKGTKNR PGSALEKEVE SMGAHLNAY STREHTAYYI KALSKDLPKA VELLADIVQN CSLEDSQIEK ERDVILQELQ ENDSSMRDVV FDYLHATAFQ G TPLAQSVE GPSENVRKLS RADLTEYVSQ HYKAPRMVLA AAGGVEHRQL LDLAQKHFSS LSGTYVEDAV PAFTPCRFTG SE IRHRDDA LPLAHVAIAV EGPGWANPDN VPLQVANAII GHYDSTYGGG THMSSTLASV AATRKLCQSF QTFNICYAET GLL GAHFVC DNMSIDDMMF FLQGQWMRLC TSATESEVVR GKNILRNALV SHLDGTTPVC EDIGRSLLTY GRRIPLAEWE SRIA EVDAS VVREVCSKYF YDQCPAVAGL GPIEQLPDYN RIRSGMFWLR F

UniProtKB: Cytochrome b-c1 complex subunit 1, mitochondrial

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Macromolecule #49: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 49 / 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 #50: Cytochrome c domain-containing protein

MacromoleculeName: Cytochrome c domain-containing protein / type: protein_or_peptide / ID: 50 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 27.373357 KDa
SequenceString: TDLELHAPSY PWSHRGLLSS LDHTSIRRGF QVYKQVCSSC HSMDYVAYRH LVGVCYTEEE AKALAEEVEV QDGPNEDGEM FMRPGKLSD YFPKPYPNPE AARAANNGAL PPDLSYIVRA RHGGEDYVFS LLTGYCEPPT GVSLREGLYF NPYFPGQAIA M APPIYNEV ...String:
TDLELHAPSY PWSHRGLLSS LDHTSIRRGF QVYKQVCSSC HSMDYVAYRH LVGVCYTEEE AKALAEEVEV QDGPNEDGEM FMRPGKLSD YFPKPYPNPE AARAANNGAL PPDLSYIVRA RHGGEDYVFS LLTGYCEPPT GVSLREGLYF NPYFPGQAIA M APPIYNEV LEFDDGTPAT MSQVAKDVCT FLRWASEPEH DHRKRMGLKM LMMMGLLLPL VYAMKRHKWS VLKSRKLAYR PP K

UniProtKB: UNIPROTKB: A0A8D0K1H3

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Macromolecule #51: Cytochrome b-c1 complex subunit Rieske, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske, mitochondrial / type: protein_or_peptide / ID: 51 / Number of copies: 3 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
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 #52: Cytochrome b-c1 complex subunit 6

MacromoleculeName: Cytochrome b-c1 complex subunit 6 / type: protein_or_peptide / ID: 52 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 7.933944 KDa
SequenceString:
ELVDPLTTVR EQCEQIEKCI KARERLELCD QRVSSRSQTE EDCTEELFDF LHARDHCVAH KLFNSLK

UniProtKB: Cytochrome b-c1 complex subunit 6

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Macromolecule #53: Cytochrome b-c1 complex subunit 7

MacromoleculeName: Cytochrome b-c1 complex subunit 7 / type: protein_or_peptide / ID: 53 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.644447 KDa
SequenceString:
SKWLEGIRKW YYNAAGFNKL GLMRDDTIYE DDDVKEAIRR LPENLYNDRV FRIKRALDLT MRQQILPKEQ WTKYEEDKFY LEPYLKEVI RERKEREEWA KK

UniProtKB: Cytochrome b-c1 complex subunit 7

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Macromolecule #54: Cytochrome b-c1 complex subunit 8

MacromoleculeName: Cytochrome b-c1 complex subunit 8 / type: protein_or_peptide / ID: 54 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.653144 KDa
SequenceString:
GREFGHLTRM RHVITYSLSP FEQRAFPHYF TKGIPNVLRR TRACILRVAP PFVVFYLVYT WGTQEFEKSK RKNPAAYEND K

UniProtKB: Cytochrome b-c1 complex subunit 8

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Macromolecule #55: Complex III subunit 9

MacromoleculeName: Complex III subunit 9 / type: protein_or_peptide / ID: 55 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 7.281334 KDa
SequenceString:
AAPTLTARLY SLLFRRTSTF ALTIAVGALF FERAFDQGAD AIYEHINQGK LWKHIKHKYE NKE

UniProtKB: Complex III subunit 9

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Macromolecule #56: Cytochrome b-c1 complex subunit 10

MacromoleculeName: Cytochrome b-c1 complex subunit 10 / type: protein_or_peptide / ID: 56 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 6.058093 KDa
SequenceString:
MLSRFLGPRY RELARNWIPT ASMWGAVGAV GLVWATDWRL ILDWVPYING KF

UniProtKB: Cytochrome b-c1 complex subunit 10

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Macromolecule #57: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

MacromoleculeName: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
type: protein_or_peptide / ID: 57 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 75.68368 KDa
SequenceString: NLIEVFVDGQ SVMVEPGTTV LQACEKVGMQ IPRFCYHERL SVAGNCRMCL VEIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVME FLLANHPLDC PICDQGGECD LQDQSMMFGS DRSRFLEGKR AVEDKNIGPL VKTIMTRCIQ CTRCIRFASE I AGVDDLGT ...String:
NLIEVFVDGQ SVMVEPGTTV LQACEKVGMQ IPRFCYHERL SVAGNCRMCL VEIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVME FLLANHPLDC PICDQGGECD LQDQSMMFGS DRSRFLEGKR AVEDKNIGPL VKTIMTRCIQ CTRCIRFASE I AGVDDLGT TGRGNDMQVG TYIEKMFMSE LSGNIIDICP VGALTSKPYA FTARPWETRK TESIDVMDAV GSNIVVSTRT GE VMRILPR MHEDINEEWI SDKTRFAYDG LKRQRLTQPM IRNEKGLLTY TTWEDALSRV AGMLQSFQGN DVAAIAGGLV DAE ALVALK DLLNRVDSDS LCTEEVFPTA GAGTDLRSNY LLNTTIAGVE EADVILLVGT NPRFEAPLFN ARIRKSWLHN DLKV ALIGS PVDLTYRYDH LGDSPKILQD IASGNHPFSQ ILKEAKKPMV VLGSSALQRS DGTAILAAVS NIAQNIRLSS GVTGD WKVM NILHRIASQV AALDLGYKPG VEAIRKNPPK VLFLLGADGG CITRQDLPKD CFIIYQGHHG DVGAPMADVI LPGAAY TEK SATYVNTEGR AQQTKVAVTP PGLAREDWKI IRALSEIAGM TLPYDTLDQV RSRLEEVSPN LVRYDDVEGA NYFQQAN EL SKLVNQQLLA DPLVPPQLTI KDFYMTDSIS RASQTMAKCV KAVTEGI

UniProtKB: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

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Macromolecule #58: Complex I-49kD

MacromoleculeName: Complex I-49kD / type: protein_or_peptide / ID: 58 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 49.234324 KDa
SequenceString: ARQWQPDVEW AEQFGGAVMY PTKETAHWKP PPWNDVDPPK DTLVSNLTLN FGPQHPAAHG VLRLVMELSG EMVRKCDPHI GLLH(2MR)GTEK LIEYKTYLQA LPYFDRLDYV SMMCNEQAYS LAVEKLLNIQ PPPRAQWIRV LFGEITRLLN HIMAVTT HA LDIGAMTPFF ...String:
ARQWQPDVEW AEQFGGAVMY PTKETAHWKP PPWNDVDPPK DTLVSNLTLN FGPQHPAAHG VLRLVMELSG EMVRKCDPHI GLLH(2MR)GTEK LIEYKTYLQA LPYFDRLDYV SMMCNEQAYS LAVEKLLNIQ PPPRAQWIRV LFGEITRLLN HIMAVTT HA LDIGAMTPFF WMFEEREKMF EFYERVSGAR MHAAYIRPGG VHQDLPLGLL DDIYEFSKNF SFRIDELEEM LTNNRIWR N RTVDIGVVTA EDALNYGFSG VMLRGSGIQW DLRKTQPYDV YDQVEFDVPI GSRGDCYDRY LCRVEEMRQS LRIISQCLN KMPPGEIKVD DAKVSPPKRA EMKTSMESLI HHFKLYTEGY QVPPGATYTA IEAPKGEFGV YLVSDGSSRP YRCKIKAPGF AHLAGLDKM SKGHMLADVV AIIGTQDIVF GEVDR

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

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Macromolecule #59: Complex I-30kD

MacromoleculeName: Complex I-30kD / type: protein_or_peptide / ID: 59 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 24.52173 KDa
SequenceString: TRPTIRPRND VVHKQLSAFG QYVAEILPKY VQQVQVSCFN ELEIFIHPDG VIPVLTFLRD HTNAQFKSLA DLTAVDVPTR QNRFEIVYN LLSLRFNSRI RVKTYTDELT PIESSVTVYK AANWYEREIW DMFGVFFANH PDLRRILTDY GFEGHPFRKD F PLSGYVEL ...String:
TRPTIRPRND VVHKQLSAFG QYVAEILPKY VQQVQVSCFN ELEIFIHPDG VIPVLTFLRD HTNAQFKSLA DLTAVDVPTR QNRFEIVYN LLSLRFNSRI RVKTYTDELT PIESSVTVYK AANWYEREIW DMFGVFFANH PDLRRILTDY GFEGHPFRKD F PLSGYVEL RYDDEVKRVV AEPVELAQEF RKFDLNSPWE AFPAYRQPPE

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

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Macromolecule #60: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 60 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.31426 KDa
SequenceString:
LIAVDEKLDI TTLTGVPEEH IKTRKVRIFV PARNNMQSGV NNTKKWKMEF DTRERWENPL MGWSSTADPL SNLVLTFSTK EDAVAFAEK NGWSFDVEER KVPKPKSKSY GANFSWNKRT RVSTK

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

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Macromolecule #61: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / type: protein_or_peptide / ID: 61 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.375395 KDa
SequenceString:
PFFDVQKRLG LDLDRWMTIQ SAEQPHKIPG RCHAFEKEWI ECAHGIGGIR AEKECKIEFD DFVECLLRQK TMKRLSAIKR QRDKLIKEG KYTPPPHHLG KEDPRP

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

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Macromolecule #62: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
type: protein_or_peptide / ID: 62 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 10.567635 KDa
SequenceString:
GVRTSPTGEK VTHTGQAYDD GDYRRVRFSD RQKEVNENFA IDLIAEQPVS EVGSRVISCD GGGGALGHPR VYINLDKETK TGTCGYCGL QFRQPHH

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

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Macromolecule #63: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
type: protein_or_peptide / ID: 63 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 17.874953 KDa
SequenceString:
SRGEYVVAKL DDLVNWARRS SLWPMTFGLA CCAVEMMHMA APRYDMDRFG VVFRASPRQS DVMIVAGTLT NKMAPALRKV YDQMPEPRY VVSMGSCANG GGYYHYSYSV VRGCDRIVPV DIYVPGCPPT AEALLYGILQ LQRKIKREKR LRIWYRR

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

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Macromolecule #64: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
type: protein_or_peptide / ID: 64 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 20.207957 KDa
SequenceString:
TYKFVNMREP SMDMKSVTDR AAQTLLWTEL VRGLGMTLSY LFREPATINY PFEKGPLSPR FRGEHALRRY PSGEERCIAC KLCEAVCPA QAITIEAEPR ADGSRRTTRY DIDMTKCIYC GFCQEACPVD AIVEGPNFEF STETHEELLY NKEKLLNNGD K WEAEIAAN IQADYLYR

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

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Macromolecule #65: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
type: protein_or_peptide / ID: 65 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 47.235789 KDa
SequenceString: TSFGSLKDED RIFTNLYGRH DWRLKGAQSR GDWYKTKEIL LKGPDWILGE VKTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNAD EGEPGTCKDR EIIRHDPHKL VEGCLVGGRA MGARAAYIYI RGEFYNEASN LQVAIREAYE AGLIGKNACG S GYDFDVFV ...String:
TSFGSLKDED RIFTNLYGRH DWRLKGAQSR GDWYKTKEIL LKGPDWILGE VKTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNAD EGEPGTCKDR EIIRHDPHKL VEGCLVGGRA MGARAAYIYI RGEFYNEASN LQVAIREAYE AGLIGKNACG S GYDFDVFV VRGAGAYICG EETALIESIE GKQGKPRLKP PFPADVGVFG CPTTVANVET VAVSPTICRR GGAWFASFGR ER NSGTKLF NISGHVNHPC TVEEEMSVPL KELIEKHAGG VIGGWDNLLA VIPGGSSTPL IPKSVCETVL MDFDALVQAQ TGL GTAAVI VMDRSTDIVK AIARLIEFYK HESCGQCTPC REGVDWMNKV MARFVKGDAR PAEIDSLWEI SKQIEGHTIC ALGD GAAWP VQGLIRHFRP ELEERMQQFA LQHQAR

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

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Macromolecule #66: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
type: protein_or_peptide / ID: 66 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 23.826336 KDa
SequenceString: GAGGALFVHR DTPENNPDTP FDFTPENYKR IEAIVKNYPE GHKAAAVLPV LDLAQRQNGW LPISAMNKVA EILQVPPMRV YEVATFYTM YNRKPVGKYH IQVCTTTPCM LRNSDSILEA IQKKLGIKVG ETTPDKLFTL IEVECLGACV NAPMVQINDN Y YEDLTPKD ...String:
GAGGALFVHR DTPENNPDTP FDFTPENYKR IEAIVKNYPE GHKAAAVLPV LDLAQRQNGW LPISAMNKVA EILQVPPMRV YEVATFYTM YNRKPVGKYH IQVCTTTPCM LRNSDSILEA IQKKLGIKVG ETTPDKLFTL IEVECLGACV NAPMVQINDN Y YEDLTPKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG PGFGVQAGL

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

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Macromolecule #67: Complex I-9kD

MacromoleculeName: Complex I-9kD / type: protein_or_peptide / ID: 67 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 5.046509 KDa
SequenceString:
DNSTYRNLQH HEYSTYTFLD LNVELSKFRM PQPSSGRQSP RH

UniProtKB: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial

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Macromolecule #68: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 68 / Number of copies: 24 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Macromolecule #69: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 69 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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: 29 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

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

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Macromolecule #71: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine

MacromoleculeName: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / type: ligand / ID: 71 / Number of copies: 27 / Formula: PEE
Molecular weightTheoretical: 744.034 Da
Chemical component information

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM

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Macromolecule #72: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 72 / Number of copies: 6 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

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

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Macromolecule #73: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 73 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

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Macromolecule #74: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...

MacromoleculeName: S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate
type: ligand / ID: 74 / Number of copies: 2 / Formula: ZMP
Molecular weightTheoretical: 568.704 Da
Chemical component information

ChemComp-ZMP:
S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate

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Macromolecule #75: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 75 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #76: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,...

MacromoleculeName: (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL
type: ligand / ID: 76 / Number of copies: 10 / Formula: PLX
Molecular weightTheoretical: 767.132 Da
Chemical component information

ChemComp-PLX:
(9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL / phospholipid*YM

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Macromolecule #77: HEME-A

MacromoleculeName: HEME-A / type: ligand / ID: 77 / Number of copies: 2 / Formula: HEA
Molecular weightTheoretical: 852.837 Da
Chemical component information

ChemComp-HEA:
HEME-A

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Macromolecule #78: COPPER (II) ION

MacromoleculeName: COPPER (II) ION / type: ligand / ID: 78 / Number of copies: 3 / Formula: CU
Molecular weightTheoretical: 63.546 Da
Chemical component information

ChemComp-CU:
COPPER (II) ION

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Macromolecule #79: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 79 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #80: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 80 / Number of copies: 4 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

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Macromolecule #81: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 81 / Number of copies: 2 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C

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Macromolecule #82: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 82 / Number of copies: 4 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

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Macromolecule #83: 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE

MacromoleculeName: 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE / type: ligand / ID: 83 / Number of copies: 1 / Formula: PX2
Molecular weightTheoretical: 535.671 Da
Chemical component information

ChemComp-PX2:
1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE

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Macromolecule #84: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 84 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER

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Macromolecule #85: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 85 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.25 mg/mL
BufferpH: 7.4
Component:
ConcentrationFormulaName
20.0 mMTrisTrimethylsilyl
50.0 mMNaClSodium chloride
0.002 %PMSFPhenylmethylsulfonyl
0.1 %GDNGlyco-diosgenin

Details: SEC buffer (20 mM Tris pH 7.4, 50 mM NaCl, 0.002% PMSF, 0.1% GDN (w/v))
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 2 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.039 kPa / Details: 15mA
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number grids imaged: 1 / Average exposure time: 7.8 sec. / Average electron dose: 51.9 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
In silico model: 3D ab-inito model reconstruction in cryosparc
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.01 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. v4.4.1) / Number images used: 250490
Initial angle assignmentType: COMMON LINE / Software - Name: cryoSPARC (ver. v4.4.1)
Final angle assignmentType: COMMON LINE / Software - Name: cryoSPARC (ver. v4.4.1)
Final 3D classificationSoftware - Name: cryoSPARC (ver. v4.4.1)
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-8zou:
Respirasome open state 2 in presence of metformin (SC-MetO2)

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