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- EMDB-13611: The acetogenin-bound complex I of Mus musculus resolved to 3.4 an... -

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Basic information

Entry
Database: EMDB / ID: EMD-13611
TitleThe acetogenin-bound complex I of Mus musculus resolved to 3.4 angstroms
Map dataGlobally sharpened map (postprocessed) in Relion
Sample
  • Complex: Mitochondrial NADH:ubiquinone oxidoreductase from Mus musculus
    • Protein or peptide: x 44 types
  • Ligand: x 11 types
Function / homology
Function and homology information


response to injury involved in regulation of muscle adaptation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / reproductive system development / Mitochondrial protein import / Respiratory electron transport / Glyoxylate metabolism and glycine degradation / RHOG GTPase cycle / respiratory system process / protein insertion into mitochondrial inner membrane ...response to injury involved in regulation of muscle adaptation / Mitochondrial Fatty Acid Beta-Oxidation / Complex I biogenesis / reproductive system development / Mitochondrial protein import / Respiratory electron transport / Glyoxylate metabolism and glycine degradation / RHOG GTPase cycle / respiratory system process / protein insertion into mitochondrial inner membrane / response to light intensity / blastocyst hatching / circulatory system development / ubiquinone-6 biosynthetic process / cellular response to oxygen levels / psychomotor behavior / mitochondrial large ribosomal subunit binding / iron-sulfur cluster assembly complex / gliogenesis / neural precursor cell proliferation / mitochondrial respirasome / NADH dehydrogenase activity / cardiac muscle tissue development / [2Fe-2S] cluster assembly / oxygen sensor activity / respiratory chain complex I / cellular respiration / negative regulation of non-canonical NF-kappaB signal transduction / adult walking behavior / ubiquinone binding / cellular response to glucocorticoid stimulus / positive regulation of mitochondrial membrane potential / acyl binding / response to hydroperoxide / mitochondrial ribosome / electron transport coupled proton transport / mitochondrial ATP synthesis coupled electron transport / iron-sulfur cluster assembly / acyl carrier activity / mitochondrial translation / adult behavior / dopamine metabolic process / NADH:ubiquinone reductase (H+-translocating) / positive regulation of ATP biosynthetic process / mitochondrial respiratory chain complex I / proton motive force-driven mitochondrial ATP synthesis / apoptotic mitochondrial changes / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / electron transport chain / NADH dehydrogenase (ubiquinone) activity / quinone binding / neuron development / ATP synthesis coupled electron transport / cellular response to interferon-beta / negative regulation of intrinsic apoptotic signaling pathway / aerobic respiration / ATP metabolic process / cellular response to retinoic acid / negative regulation of reactive oxygen species biosynthetic process / extrinsic apoptotic signaling pathway / response to cAMP / response to organonitrogen compound / tricarboxylic acid cycle / respiratory electron transport chain / ionotropic glutamate receptor binding / reactive oxygen species metabolic process / visual perception / Neutrophil degranulation / cerebellum development / neurogenesis / mitochondrion organization / response to hormone / fatty acid metabolic process / response to cocaine / regulation of mitochondrial membrane potential / response to nicotine / muscle contraction / synaptic membrane / kidney development / apoptotic signaling pathway / mitochondrial membrane / sensory perception of sound / regulation of protein phosphorylation / brain development / multicellular organism growth / response to hydrogen peroxide / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / negative regulation of cell growth / response to organic cyclic compound / cognition / circadian rhythm / positive regulation of protein catabolic process / NAD binding / positive regulation of fibroblast proliferation / FMN binding / myelin sheath / nervous system development / 4 iron, 4 sulfur cluster binding
Similarity search - Function
NmrA-like domain / NmrA-like family / Complex1_LYR-like / 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) / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1, NDUB1 ...NmrA-like domain / NmrA-like family / Complex1_LYR-like / 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) / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1, NDUB1 / MNLL subunit / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH-ubiquinone oxidoreductase, subunit 10 / NADH-ubiquinone oxidoreductase subunit 10 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase MWFE subunit / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / Zinc finger, CHCC-type / Zinc-finger domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, metazoa / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, animal type / NADH:ubiquinone oxidoreductase subunit B14.5a (Complex I-B14.5a) / NADH dehydrogenase 1 beta subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 / NADH dehydrogenase 1 alpha subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] 1 subunit C2, NDUC2 / NADH:ubiquinone oxidoreductase, subunit NDUFB4 / NADH-ubiquinone oxidoreductase subunit b14.5b (NDUFC2) / NADH-ubiquinone oxidoreductase B15 subunit (NDUFB4) / NADH dehydrogenase 1, beta subcomplex, subunit 6 / NADH:ubiquinone oxidoreductase, NDUFB6/B17 subunit / NADH:ubiquinone oxidoreductase chain 4, N-terminal / NADH:ubiquinone oxidoreductase, chain 2 / NADH dehydrogenase subunit 2, C-terminal / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / NADH:ubiquinone oxidoreductase, NDUFB5/SGDH subunit / NADH-ubiquinone oxidoreductase chain 4, amino terminus / NADH dehydrogenase subunit 2 C-terminus / NADH:ubiquinone oxidoreductase, NDUFB5/SGDH subunit / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8 / GRIM-19 / NADH-ubiquinone oxidoreductase ASHI subunit (CI-ASHI or NDUFB8) / GRIM-19 protein / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase subunit 5, C-terminal / NADH dehydrogenase subunit 5 C-terminus / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / NADH-ubiquinone oxidoreductase B12 subunit family / NDUFA6, LYR domain / NADH:ubiquinone oxidoreductase, NDUFS5-15kDa / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7, NDUB7 / NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7) / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NDUFB9, LYR domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH:ubiquinone oxidoreductase, iron-sulphur subunit 5 / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 8 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / Deoxynucleoside kinase domain / Deoxynucleoside kinase / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH dehydrogenase, subunit C / NADH ubiquinone oxidoreductase, F subunit / NADH-plastoquinone oxidoreductase, chain 5 subgroup / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / NADH-quinone oxidoreductase, chain M/4 / Complex 1 LYR protein domain / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH-ubiquinone oxidoreductase chain 4L/K / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / Complex 1 protein (LYR family) / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-quinone oxidoreductase, chain 5-like / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 2 / NADH-ubiquinone oxidoreductase chain 3 / NADH-ubiquinone oxidoreductase chain 4L / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 6 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 ...NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 / NADH-ubiquinone oxidoreductase chain 1 / NADH-ubiquinone oxidoreductase chain 2 / NADH-ubiquinone oxidoreductase chain 3 / NADH-ubiquinone oxidoreductase chain 4L / NADH-ubiquinone oxidoreductase chain 4 / NADH-ubiquinone oxidoreductase chain 5 / NADH-ubiquinone oxidoreductase chain 6 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial / NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 subunit C2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 / NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 / Acyl carrier protein, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
Similarity search - Component
Biological speciesMus musculus (house mouse) / house mouse (house mouse) / Mouse (mice)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsGrba D / Hirst J
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MC_U105663141 United Kingdom
Medical Research Council (MRC, United Kingdom)MC_UU_00015/2 United Kingdom
CitationJournal: J Biol Chem / Year: 2022
Title: Cryo-electron microscopy reveals how acetogenins inhibit mitochondrial respiratory complex I.
Authors: Daniel N Grba / James N Blaza / Hannah R Bridges / Ahmed-Noor A Agip / Zhan Yin / Masatoshi Murai / Hideto Miyoshi / Judy Hirst /
Abstract: Mitochondrial complex I (NADH:ubiquinone oxidoreductase), a crucial enzyme in energy metabolism, captures the redox potential energy from NADH oxidation/ubiquinone reduction to create the proton ...Mitochondrial complex I (NADH:ubiquinone oxidoreductase), a crucial enzyme in energy metabolism, captures the redox potential energy from NADH oxidation/ubiquinone reduction to create the proton motive force used to drive ATP synthesis in oxidative phosphorylation. High-resolution single-particle electron cryo-EM analyses have provided detailed structural knowledge of the catalytic machinery of complex I, but not of the molecular principles of its energy transduction mechanism. Although ubiquinone is considered to bind in a long channel at the interface of the membrane-embedded and hydrophilic domains, with channel residues likely involved in coupling substrate reduction to proton translocation, no structures with the channel fully occupied have yet been described. Here, we report the structure (determined by cryo-EM) of mouse complex I with a tight-binding natural product acetogenin inhibitor, which resembles the native substrate, bound along the full length of the expected ubiquinone-binding channel. Our structure reveals the mode of acetogenin binding and the molecular basis for structure-activity relationships within the acetogenin family. It also shows that acetogenins are such potent inhibitors because they are highly hydrophobic molecules that contain two specific hydrophilic moieties spaced to lock into two hydrophilic regions of the otherwise hydrophobic channel. The central hydrophilic section of the channel does not favor binding of the isoprenoid chain when the native substrate is fully bound but stabilizes the ubiquinone/ubiquinol headgroup as it transits to/from the active site. Therefore, the amphipathic nature of the channel supports both tight binding of the amphipathic inhibitor and rapid exchange of the ubiquinone/ubiquinol substrate and product.
History
DepositionSep 22, 2021-
Header (metadata) releaseApr 6, 2022-
Map releaseApr 6, 2022-
UpdateApr 6, 2022-
Current statusApr 6, 2022Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_13611.png

Downloads & links

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Map

FileDownload / File: emd_13611.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationGlobally sharpened map (postprocessed) in Relion
Voxel sizeX=Y=Z: 1.043 Å
Density
Contour LevelBy AUTHOR: 0.035
Minimum - Maximum-0.08404521 - 0.26540214
Average (Standard dev.)-4.7450998e-05 (±0.00802398)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions450450450
Spacing450450450
CellA=B=C: 469.35 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_13611_msk_1.map
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Additional map: Unfiltered consensus map from Relion

Fileemd_13611_additional_1.map
AnnotationUnfiltered consensus map from Relion
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Additional map: Locally sharpened map using LocalDeblur

Fileemd_13611_additional_2.map
AnnotationLocally sharpened map using LocalDeblur
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Half map: Half map 1

Fileemd_13611_half_map_1.map
AnnotationHalf map 1
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Half map: Half map 2

Fileemd_13611_half_map_2.map
AnnotationHalf map 2
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Sample components

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Entire : Mitochondrial NADH:ubiquinone oxidoreductase from Mus musculus

EntireName: Mitochondrial NADH:ubiquinone oxidoreductase from Mus musculus
Components
  • Complex: Mitochondrial NADH:ubiquinone oxidoreductase from Mus musculus
    • 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 dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
    • 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: Acyl carrier protein, mitochondrial
    • 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: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
    • 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
    • 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 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 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 7
    • 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
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: (3~{S},5~{S})-5-methyl-3-[(13~{R})-13-oxidanyl-13-[(2~{R},5~{R})-5-[(2~{R},5~{R})-5-[(1~{R})-1-oxidanylundecyl]oxolan-2-yl]oxolan-2-yl]tridecyl]oxolan-2-one
  • Ligand: CARDIOLIPIN
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • 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

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Supramolecule #1: Mitochondrial NADH:ubiquinone oxidoreductase from Mus musculus

SupramoleculeName: Mitochondrial NADH:ubiquinone oxidoreductase from Mus musculus
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#44
Details: Solubilised in DDM detergent. Native purification via anion exchange, with inhibitor acetogenin added, and size-exclusion chromatography.
Source (natural)Organism: Mus musculus (house mouse)

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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: house mouse (house mouse)
Molecular weightTheoretical: 13.251785 KDa
SequenceString:
(FME)NLYTVIFIN ILLSLTLILV AFWLPQMNLY SEKANPYECG FDPTSSARLP FSMKFFLVAI TFLLFDLEIA LLLPLP WAI QTIKTSTMMI MAFILVTILS LGLAYEWTQK GLEWTE

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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 / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 24.715912 KDa
SequenceString: MAALAAPGLL SVRILGLRTA QVQLRRVHQS VATEGPSPSP SPSLSSTQSA VSKAGAGAVV PKLSHLPRSR AEYVVTKLDD LINWARRSS LWPMTFGLAC CAVEMMHMAA PRYDMDRFGV VFRASPRQAD VMIVAGTLTN KMAPALRKVY DQMPEPRYVV S MGSCANGG ...String:
MAALAAPGLL SVRILGLRTA QVQLRRVHQS VATEGPSPSP SPSLSSTQSA VSKAGAGAVV PKLSHLPRSR AEYVVTKLDD LINWARRSS LWPMTFGLAC CAVEMMHMAA PRYDMDRFGV VFRASPRQAD VMIVAGTLTN KMAPALRKVY DQMPEPRYVV S MGSCANGG GYYHYSYSVV RGCDRIVPVD IYVPGCPPTA EALLYGILQL QRKIKREQKL KIWYRR

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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 / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 30.191307 KDa
SequenceString: MAAAAARVWC RGLLGAASVG RGAGRPSVLW QHVRRESAAA DKRPTVRPRS DVTHKQLSAF GEYVAEILPK YVQQVQVSCL DELEICIHP DGVIPTLTFL RDHTNAQFKS LADLTAVDVP TRQNRFEIVY NLLSLRFNSR IRVKTYADEL TPIDSIVSVH I AANWYERE ...String:
MAAAAARVWC RGLLGAASVG RGAGRPSVLW QHVRRESAAA DKRPTVRPRS DVTHKQLSAF GEYVAEILPK YVQQVQVSCL DELEICIHP DGVIPTLTFL RDHTNAQFKS LADLTAVDVP TRQNRFEIVY NLLSLRFNSR IRVKTYADEL TPIDSIVSVH I AANWYERE VWDMFGVFFF NHPDLRRILT DYGFEGHPFR KDFPLTGYVE LRYDDEVKRV VAEPVELAQE FRKFDLNSPW EA FPAYRQP PESLKLEAGD KKPETK

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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 / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 52.720602 KDa
SequenceString: MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH WKPPPWNDVD ILKEKAVTNM TLNFGPQHP AAHGVLRLVL ELSGEMVRKC DPHIGLLH(2MR)G TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSIAVE KL LNIQPPPRAQ ...String:
MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH WKPPPWNDVD ILKEKAVTNM TLNFGPQHP AAHGVLRLVL ELSGEMVRKC DPHIGLLH(2MR)G TEKLIEYKTY LQALPYFDRL DYVSMMCNEQ AYSIAVE KL LNIQPPPRAQ WIRVLFGEIT RILNHIMAVT THALDIGAMT PFFWMFEERE KMFEFYERVS GARMHAAYIR PGGVHQDL P LGLLDDIYEF SKNFSLRIDE VEEMLTNNRI WRNRTVDIGV VTAEDALNYG FSGVMLRGSG IQWDLRKTQP YDVYDQVEF DVPIGSRGDC YDRYLCRVEE MRQSLRIIEQ CLNKMPPGEI KVDDAKVSPP KRAEMKTSME SLIHHFKLYT EGYQVPPGAT YTAIEAPKG EFGVYLVSDG SSRPYRCKIK APGFAHLAGL DKMSKGHMLA DVVAIIGTQD IVFGEIDR

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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 / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 27.318336 KDa
SequenceString: MFSLALRARA TGLAAQWGRH ARNLHKTAVH NGAGGALFVH RDTPENNPDT PFDFTPENYK RIEAIVKNYP EGHQAAAVLP VLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT MYNRKPVGKY HIQVCTTTPC MLRDSDSILE TLQRKLGIKV G ETTPDKLF ...String:
MFSLALRARA TGLAAQWGRH ARNLHKTAVH NGAGGALFVH RDTPENNPDT PFDFTPENYK RIEAIVKNYP EGHQAAAVLP VLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT MYNRKPVGKY HIQVCTTTPC MLRDSDSILE TLQRKLGIKV G ETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTPK DIEEIIDELK AGKVPKPGPR SGRFCCEPAG GLTSLTEPPK GP GFGVQAG L

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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 / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 50.904152 KDa
SequenceString: MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG DWYKTKEILL KGPDWILGEM KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IMRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN ...String:
MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG DWYKTKEILL KGPDWILGEM KTSGLRGRG GAGFPTGLKW SFMNKPSDGR PKYLVVNADE GEPGTCKDRE IMRHDPHKLV EGCLVGGRAM GARAAYIYIR G EFYNEASN LQVAIREAYE AGLIGKNACG SDYDFDVFVV RGAGAYICGE ETALIESIEG KQGKPRLKPP FPADVGVFGC PT TVANVET VAVSPTICRR GGTWFAGFGR ERNSGTKLFN ISGHVNHPCT VEEEMSVPLK ELIEKHAGGV TGGWDNLLAV IPG GSSTPL IPKSVCETVL MDFDALVQAQ TGLGTAAVIV MDRSTDIVKA IARLIEFYKH ESCGQCTPCR EGVDWMNKVM ARFV KGDAR PAEIDSLWEI SKQIEGHTIC ALGDGAAWPV QGLIRHFRPE LEDRMQRFAQ QHRAWQAAS

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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 / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 79.866688 KDa
SequenceString: MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL ...String:
MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVV AACAMPVMKG WNILTNSEKS KKAREGVMEF LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFLEGKRA V EDKNIGPL VKTIMTRCIQ CTRCIRFASE IAGVDDLGTT GRGNDMQVGT YIEKMFMSEL SGNVIDICPV GALTSKPYAF TA RPWETRK TESIDVMDAV GSNIVVSTRT GEVMRILPRM HEDINEEWIS DKTRFAYDGL KRQRLTEPMV RNEKGLLTYT SWE DALSRV AGMLQNFEGN AVAAIAGGLV DAEALVALKD LLNKVDSDNL CTEEIFPTEG AGTDLRSNYL LNTTIAGVEE ADVV LLVGT NPRFEAPLFN ARIRKSWLHN DLKVALIGSP VDLTYRYDHL GDSPKILQDI ASGRHSFCEV LKDAKKPMVV LGSSA LQRD DGAAILVAVS NMVQKIRVTT GVAAEWKVMN ILHRIASQVA ALDLGYKPGV EAIRKNPPKM LFLLGADGGC ITRQDL PKD CFIVYQGHHG DVGAPMADVI LPGAAYTEKS ATYVNTEGRA QQTKVAVTPP GLAREDWKII RALSEIAGIT LPYDTLD QV RNRLEEVSPN LVRYDDIEET NYFQQASELA KLVNQEVLAD PLVPPQLTIK DFYMTDSISR ASQTMAKCVK AVTEGAQA V EEPSIC

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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: house mouse (house mouse)
Molecular weightTheoretical: 36.105027 KDa
SequenceString: (FME)FFINILTLL VPILIAMAFL TLVERKILGY MQLRKGPNIV GPYGILQPFA DAMKLFMKEP MRPLTTSMSL FIIAPT LSL TLALSLWVPL PMPHPLINLN LGILFILATS SLSVYSILWS GWASNSKYSL FGALRAVAQT ISYEVTMAII LLSVLLM NG SYSLQTLITT ...String:
(FME)FFINILTLL VPILIAMAFL TLVERKILGY MQLRKGPNIV GPYGILQPFA DAMKLFMKEP MRPLTTSMSL FIIAPT LSL TLALSLWVPL PMPHPLINLN LGILFILATS SLSVYSILWS GWASNSKYSL FGALRAVAQT ISYEVTMAII LLSVLLM NG SYSLQTLITT QEHMWLLLPA WPMAMMWFIS TLAETNRAPF DLTEGESELV SGFNVEYAAG PFALFFMAEY TNIILMNA L TTIIFLGPLY YINLPELYST NFMMEALLLS STFLWIRASY PRFRYDQLMH LLWKNFLPLT LALCMWHISL PIFTAGVPP YM

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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 / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 24.068355 KDa
SequenceString: MYRLSSSMLP RALAQAMRTG HLNGQSLHSS AVAATYKYVN KKEQESEVDM KSATDNAARI LMWTELIRGL GMTLSYLFRE PATINYPFE KGPLSPRFRG EHALRRYPSG EERCIACKLC EAICPAQAIT IEAEPRADGS RRTTRYDIDM TKCIYCGFCQ E ACPVDAIV ...String:
MYRLSSSMLP RALAQAMRTG HLNGQSLHSS AVAATYKYVN KKEQESEVDM KSATDNAARI LMWTELIRGL GMTLSYLFRE PATINYPFE KGPLSPRFRG EHALRRYPSG EERCIACKLC EAICPAQAIT IEAEPRADGS RRTTRYDIDM TKCIYCGFCQ E ACPVDAIV EGPNFEFSTE THEELLYNKE KLLNNGDKWE AEIAANIQAD YLYR

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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 / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 18.6561 KDa
SequenceString:
(FME)NNYIFVLSS LFLVGCLGLA LKPSPIYGGL GLIVSGFVGC LMVLGFGGSF LGLMVFLIYL GGMLVVFGYT TAMATE EYP ETWGSNWLIL GFLVLGVIME VFLICVLNYY DEVGVINLDG LGDWLMYEVD DVGVMLEGGI GVAAMYSCAT WMMVVAG WS LFAGIFIIIE ITRD

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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: house mouse (house mouse)
Molecular weightTheoretical: 10.637629 KDa
SequenceString:
(FME)PSTFFNLTM AFSLSLLGTL MFRSHLMSTL LCLEGMVLSL FIMTSVTSLN SNSMSSMPIP ITILVFAACE AAVGLA LLV KVSNTYGTDY VQNLNLLQC

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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: Mouse (mice)
Molecular weightTheoretical: 68.547297 KDa
SequenceString: (FME)NIFTTSILL IFILLLSPIL ISMSNLIKHI NFPLYTTTSI KFSFIISLLP LLMFFHNNME YMITTWHWVT MNSMEL KMS FKTDFFSILF TSVALFVTWS IMQFSSWYMH SDPNINRFIK YLTLFLITML ILTSANNMFQ LFIGWEGVGI MSFLLIG WW YGRTDANTAA ...String:
(FME)NIFTTSILL IFILLLSPIL ISMSNLIKHI NFPLYTTTSI KFSFIISLLP LLMFFHNNME YMITTWHWVT MNSMEL KMS FKTDFFSILF TSVALFVTWS IMQFSSWYMH SDPNINRFIK YLTLFLITML ILTSANNMFQ LFIGWEGVGI MSFLLIG WW YGRTDANTAA LQAILYNRIG DIGFILAMVW FSLNMNSWEL QQIMFSNNND NLIPLMGLLI AATGKSAQFG LHPWLPSA M EGPTPVSALL HSSTMVVAGI FLLVRFHPLT TNNNFILTTM LCLGALTTLF TAICALTQND IKKIIAFSTS SQLGLMMVT LGMNQPHLAF LHICTHAFFK AMLFMCSGSI IHSLADEQDI RKMGNITKIM PFTSSCLVIG SLALTGMPFL TGFYSKDLII EAINTCNTN AWALLITLIA TSMTAMYSMR IIYFVTMTKP RFPPLISINE NDPDLMNPIK RLAFGSIFAG FVISYNIPPT S IPVLTMPW FLKTTALIIS VLGFLIALEL NNLTMKLSMN KANPYSSFST LLGFFPSIIH RITPMKSLNL SLKTSLTLLD LI WLEKTIP KSTSTLHTNM TTLTTNQKGL IKLYFMSFLI NIILIIILYS INLE

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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: house mouse (house mouse)
Molecular weightTheoretical: 51.943547 KDa
SequenceString: (FME)LKIILPSLM LLPLTWLSSP KKTWTNVTSY SFLISLTSLT LLWQTDENYK NFSNMFSSDP LSTPLIILTA WLLPLM LMA SQNHLKKDNN VLQKLYISML ISLQILLIMT FSATELIMFY ILFEATLIPT LIIITRWGNQ TERLNAGIYF LFYTLIG SI PLLIALILIQ ...String:
(FME)LKIILPSLM LLPLTWLSSP KKTWTNVTSY SFLISLTSLT LLWQTDENYK NFSNMFSSDP LSTPLIILTA WLLPLM LMA SQNHLKKDNN VLQKLYISML ISLQILLIMT FSATELIMFY ILFEATLIPT LIIITRWGNQ TERLNAGIYF LFYTLIG SI PLLIALILIQ NHVGTLNLMI LSFTTHTLDA SWSNNLLWLA CMMAFLIKMP LYGVHLWLPK AHVEAPIAGS MILAAILL K LGSYGMIRIS IILDPLTKYM AYPFILLSLW GMIMTSSICL RQTDLKSLIA YSSVSHMALV IASIMIQTPW SFMGATMLM IAHGLTSSLL FCLANSNYER IHSRTMIMAR GLQMVFPLMA TWWLMASLAN LALPPSINLM GELFITMSLF SWSNFTIILM GINIIITGM YSMYMIITTQ RGKLTNHMIN LQPSHTRELT LMALHMIPLI LLTTSPKLIT GLTM

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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: Mouse (mice)
Molecular weightTheoretical: 38.80023 KDa
SequenceString: (FME)NPITLAIIY FTIFLGPVIT MSSTNLMLMW VGLEFSLLAI IPMLINKKNP RSTEAATKYF VTQATASMII LLAIVL NYK QLGTWMFQQQ TNGLILNMTL MALSMKLGLA PFHFWLPEVT QGIPLHMGLI LLTWQKIAPL SILIQIYPLL NSTIILM LA ITSIFMGAWG ...String:
(FME)NPITLAIIY FTIFLGPVIT MSSTNLMLMW VGLEFSLLAI IPMLINKKNP RSTEAATKYF VTQATASMII LLAIVL NYK QLGTWMFQQQ TNGLILNMTL MALSMKLGLA PFHFWLPEVT QGIPLHMGLI LLTWQKIAPL SILIQIYPLL NSTIILM LA ITSIFMGAWG GLNQTQMRKI MAYSSIAHMG WMLAILPYNP SLTLLNLMIY IILTAPMFMA LMLNNSMTIN SISLLWNK T PAMLTMISLM LLSLGGLPPL TGFLPKWIII TELMKNNCLI MATLMAMMAL LNLFFYTRLI YSTSLTMFPT NNNSKMMTH QTKTKPNLMF STLAIMSTMT LPLAPQLIT

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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: Mouse (mice)
Molecular weightTheoretical: 40.657375 KDa
SequenceString: MALRLLRLVP ASAPARGLAA GAQRVGRIHT SVHCKLRYGL LAAILGDKTT KKLHEYSRVI TVDGNICSGK NKLAKEIAQQ LGMKHYPEA GIQYSSTTTG DGRPLDIEFS GSCSLEKFYD DPKSNDGNSY RLQSWLYASR LLQYADALEH LLSTGQGVVL E RSIYSDFV ...String:
MALRLLRLVP ASAPARGLAA GAQRVGRIHT SVHCKLRYGL LAAILGDKTT KKLHEYSRVI TVDGNICSGK NKLAKEIAQQ LGMKHYPEA GIQYSSTTTG DGRPLDIEFS GSCSLEKFYD DPKSNDGNSY RLQSWLYASR LLQYADALEH LLSTGQGVVL E RSIYSDFV FLEAMYNQGY IRKQCVDHYN EIKRLTLPEY LPPHAVIYID VPVPEVQSRI QKKGDPHEMK VTSAYLQDIE NA YKKTFLP KMSEMCEVLV YDSWEAEDPT KVVEDIEYLK YNKGPWLKQD DWTFHYLRML VQDKTEVLNY TTIPVYLPEI TIG AHQGSR IYNSFRELPG RKYAPGYNAE VGDKWIWLK

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Macromolecule #16: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 42.588129 KDa
SequenceString: MAAAVRFRVV RALPMSRPAI TAAATSVFCG SSHRQLHHAV IPHGKGGRSS VSGVVATVFG ATGFLGRYVV NHLGRMGSQV IIPYRCDVY DIMHLRLMGD LGQLTFLEWD ARDKDSIRKA VQHSNVVINL IGREWETRNF DFEDVFVNIP RAIAQASKEA G VERFIHVS ...String:
MAAAVRFRVV RALPMSRPAI TAAATSVFCG SSHRQLHHAV IPHGKGGRSS VSGVVATVFG ATGFLGRYVV NHLGRMGSQV IIPYRCDVY DIMHLRLMGD LGQLTFLEWD ARDKDSIRKA VQHSNVVINL IGREWETRNF DFEDVFVNIP RAIAQASKEA G VERFIHVS HLNASMKSSS KSLRSKAVGE KEVRSVFPEA IIIRPSDIFG REDRFLNHFA NYRWFLAVPL VSLGFKTVKQ PV YVADVSK GIVNATKDPD AVGKTFAFTG PNRYLLFHLV KYIFGMTHRT FIPYPLPLFV YSWIGKLFGL SPFEPWTTKD KVE RIHISD VMPTDLPGLE DLGVQPTPLE LKSIEVLRRH RTYRWLSSEI EETKPAKTVN Y

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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: Mouse (mice)
Molecular weightTheoretical: 19.814725 KDa
SequenceString:
MAAVSISVSL RQAMLGRRAM ATAAVSVCRV PSRLLSTSTW KLADNQTRDT QLITVDEKLD ITTLTGVPEE HIKTRKVRIF VPARNNMQS GVNNTKKWKM EFDTRERWEN PLMGWASTAD PLSNMVLTFS AKEDAIAFAE KNGWSYDVEE KKVPKPKSKS Y GANFSWNK RTRVSTK

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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: Mouse (mice)
Molecular weightTheoretical: 13.041828 KDa
SequenceString:
MAAVLTFRRL LTLPRAARGF GVQVSPSGEK ITHTGQVYDE KDYRRVRFVD RQKEVNENFA IDLIAQQPVN EVEHRIIACD GGGGALGHP KVYINLDKET KTGTCGYCGL QFKQHHH

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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: Mouse (mice)
Molecular weightTheoretical: 10.932675 KDa
SequenceString:
MAAAAASRAV GAKLGLREIR VHLCQRSPGS QGVRDFIVQR YVELKKAHPN LPILIRECSE VQPKLWARYA FGQEKTVSLN NLSADEVTR AMQNVLSGKA

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Macromolecule #20: Acyl carrier protein, mitochondrial

MacromoleculeName: Acyl carrier protein, mitochondrial / type: protein_or_peptide / ID: 20 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 17.390289 KDa
SequenceString:
MASRVLCACV RRLPAAFAPL PRLPTLALAR PLSTTLCPEG IRRRPGALQS ALALAQVPGT VTHLCRQYSD APPLTLDGIK DRVLYVLKL YDKIDPEKLS VNSHFMKDLG LDSLDQVEII MAMEDEFGFE IPDIDAEKLM CPQEIVDYIA DKKDVYE

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 13.380719 KDa
SequenceString:
MAGLLKKTTG LVGLAVCDTP HERLTILYTK TLDILKHFPK HAAYRKYTEQ ITNEKLDMVK AEPDVKKLEA LLQGGEVEEV ILQAEKELS LARKMLKWKP WEPLVEEPPA NQWKWPI

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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: Mouse (mice)
Molecular weightTheoretical: 15.311858 KDa
SequenceString:
MAAAATGLRQ AAAAAASTSV KPIFSRDLNE AKRRVRELYR AWYREVPNTV HLMQLDITVK QGRDKVREMF MKNAHVTDPR VVDLLVIKG KMELQETIKV WKQRTHVMRF FHETETPRPK DFLSKFYMGH DP

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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: Mouse (mice)
Molecular weightTheoretical: 20.025127 KDa
SequenceString:
MPGIVELPTL EELKVEEVKV SSAVLKAAAH HYGAQCDKTN KEFMLCRWEE KDPRRCLKEG KLVNGCALNF FRQIKSHCAE PFTEYWTCL DYSNMQLFRH CRQQQAKFDQ CVLDKLGWVR PDLGQLSKVT KVKTDRPLPE NPYHSRARPE PNPVIEGDLK P AKHGTRFF FWTV

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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: Mouse (mice)
Molecular weightTheoretical: 15.130416 KDa
SequenceString:
MAMVKRFFES YHEVPDGTQC HRKTYITTAL GGICGIIGSA YSVSLNPADS TLEAVARVGR YTFTAAAIGA MFGLTTCVSA QVREKPDDP LNYFIGGCAG GLTLGARTHS YGTAAMGCVY MGTAAALFKI GKLEGWELFP TPKV

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Macromolecule #25: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 16.881588 KDa
SequenceString:
MAASKVKQDM PPPGGYGPID YKRNLPRRGL SGYSMFAVGI GALIFGYWRM MRWNQERRRL LIEDLEARIA LMPLFQAEKD RRTLQILRE NLEEEAIIMK DVPNWKVGES VFHTTRWVPP LIGEMYGLRT KEEMSNANFG FTWYT

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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: Mouse (mice)
Molecular weightTheoretical: 8.149524 KDa
SequenceString:
MWFEILPGLA IMGVCLVIPG VSTAYIHKFT NGGKEKRVAR VQYQWYLMER DRRISGVNRY YVSKGLENID

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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: Mouse (mice)
Molecular weightTheoretical: 9.338867 KDa
SequenceString:
MAGRISAFLK NAWAKEPVLV VSFSVWGLAI IMPMISPYTK YASMINKATP YNYPVPVRDD GNMPDVPSHP QDPLGPSLDW LKNL

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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: Mouse (mice)
Molecular weightTheoretical: 8.636023 KDa
SequenceString:
MAPSVVLRSF SRLLAPARLP SCSSTRSKFY VREPVNAKPN WLAVGLSVGA SVFMWIYLIQ THNEDVLEYK RRNGLE

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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: house mouse (house mouse)
Molecular weightTheoretical: 14.185692 KDa
SequenceString:
MMNGRPGHEP LKFLPDEARS LPPPKLNDPR LVYMGLLGYC TGLMDNMLRM RPVMRAGLHR QLLFVTSFVF AGYFYLKRQN YLYAVKDHD MFGYIKLHPE DFPEKEKKTY AEILEPFHPV R

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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: Mouse (mice)
Molecular weightTheoretical: 12.675772 KDa
SequenceString:
MPFLDIQKKL GISLDRHFMF LSAEQPYKNA ARCHAFEKEW IECAHGIGGT RAKKECKIEF DDFEECLLRY KTMRRMHDIK KQREKLMKE GKYTPPPHHS GREEPRP

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

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 6.965109 KDa
SequenceString:
MTLFQLLREH WVHILVPAGF VFGCYLDRKD DEKLTAFRNK SMLFQRELRP NEEVTWK

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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: Mouse (mice)
Molecular weightTheoretical: 17.463727 KDa
SequenceString:
MAARLLSLYG RCLSAAGAMR GLPAARVRWE SSRAVIAPSG VEKKRQREPT MQWQEDPEPE DENVYAKNPD FHGYDSDPVV DVWNMRAVF FFGFSIVLVF GTTFVAYVPD YRMQEWARRE AERLVKYREV NGLPIMESNY FDPSKIQLPE DD

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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: Mouse (mice)
Molecular weightTheoretical: 21.742197 KDa
SequenceString:
MAAMSLLQRA SVSALTALSC RRAGPRLGVG SFLTRSFPKT VAPVRHSGDH GKRLFVVKPS LYYDARFLRL MKFYLMLTGI PVIIGITLV NIFIGEAELA EIPEGYIPEH WEYYKHPISR WIARNFYDGP EKNYEKTLAI LQIESEKAEL RLKEQEVRRL M RARGDGPW YQFPTPEKEF IDHSPKATPD N

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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: Mouse (mice)
Molecular weightTheoretical: 15.540085 KDa
SequenceString:
MSGYTPDEKL RLQQLRELRR RWLKDQELSP REPVLPPRRM WPLERFWDNF LRDGAVWKNM VFKAYRSSLF AVSHVLIPMW FVHYYVKYH MATKPYTIVS SKPRIFPGDT ILETGEVIPP MRDFPDQHH

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Macromolecule #35: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mito...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial
type: protein_or_peptide / ID: 35 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mouse (mice)
Molecular weightTheoretical: 11.982437 KDa
SequenceString:
MSALTRLVPF GRVGGRLLRG CRARAAGDSG VRHAGGGVHI QPRYREFPQL TRSQVIQGEF LSSLMWFWIL WRFWHDSDAV LGHFSYPDP SQWTDEELGI PPDDED

+
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: Mouse (mice)
Molecular weightTheoretical: 11.71424 KDa
SequenceString:
MAAGHGHEHG HEHGHGHGKM ELPDYRQWKI EGTPLETVQK KLAARGLRDP WARNEAWRYM GGFAGNITFP SVILKGFKWG FAAFVVALG AEYFLDSQNG DKKHH

+
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: Mouse (mice)
Molecular weightTheoretical: 21.903828 KDa
SequenceString:
MAAARAAALG VRWLQRTTRG VVPLEARRAF HMTKDMLPGS YPRTPEERAA AAKKYNMRVE DYEPYPDDGM GYGDYPMLPN RSQHERDPW YQWDHSELRM NWGEPIHWDL DMYIRNRVDT SPTPVSWDVM CKHLFGFVAF MVFMFWVGHV FPSYQPVGPK Q YPYNNLYL ERGGDPTKEP EPVVHYDI

+
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: Mouse (mice)
Molecular weightTheoretical: 15.105287 KDa
SequenceString:
MSGSKYKPAP LATLPSTLDP AEYDVSPETR RAQVERLSIR ARLKREYLLQ YNDPKRVSHI EDPALIRWTY ARSANIYPNF RPTPKNSLL GAVAGFGPLI FWYYVFKTDR DRKERLIQEG KLDRKFNISY

+
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: Mouse (mice)
Molecular weightTheoretical: 22.020123 KDa
SequenceString:
MAFCAPPAYL THQQKVLRLY KRALRHLESW CIHRDKYRYF ACLMRARFEE HKNEKDMMRA TQLLREAEEE FWQNQHPQPY IFPDSPGGT SFERYECYKV PEWCLDYWHP SEKAMYPDYF SKREQWKKLR MESWDREVKQ LQEETSPDGI MTEALPPARR E GDLPPLWW HIVTRPRERP T

+
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: Mouse (mice)
Molecular weightTheoretical: 16.360804 KDa
SequenceString:
MGAHLTRRYL WDASVEPDPE KIPSFPPDLG FPERKERVMV ATQQEMMDAQ LTLQQRDYCA HYLIRLLKCK RDSFPNFLAC KHEQHDWDY CEHLDYVKRM KEFERERRLL QRKKRRALKE ARVAQGQGEG EVGPEVAL

+
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: Mouse (mice)
Molecular weightTheoretical: 21.054832 KDa
SequenceString:
MPDSWDKDVY PEPPSRTPAP SPQTSLPNPI TYLTKAYDLV VDWPVTLVRE FIERQHAKNR TYYYHRQYRR VPDITECKEG DVLCIYEAE MQWRRDFKVD QEIMNIIQER LKACQQREGE NYQQNCAKEL EQFTKVTKAY QDRYLDLGAY YSARKCLAKQ K QRMLEERK AARQEAAA

+
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: Mouse (mice)
Molecular weightTheoretical: 17.154453 KDa
SequenceString:
(AME)ELVEVLKRG VQQVTGHGGL RGLLRVFFRA NDIRIGTLVG EDKYGNKYYE DNKQFFGRHR WVIYTTEMNG KNTFWD VDG SMVPPEWHRW LHCMTDDPPT TNPPTARKFI WTNHKFNVSA TPEQYVPYST TRKKIHEWVP PSTPYK

+
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: Mouse (mice)
Molecular weightTheoretical: 12.637629 KDa
SequenceString:
M(AYA)SATRVIQK LRNWASGQDL QAKLQLRYQE IAKRTQPPPK LPVGPSHKLS NNYYCTRDGR REVVPPSIIM SSQKAL VSG KAAESSAMAA TEKKAVTPAP PMKRWELSKD QPYL

+
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: Mouse (mice)
Molecular weightTheoretical: 11.833504 KDa
SequenceString:
MAVSLLLRGG RIRALKAVLL EARVFPGELV SVVRLSTESE KSAKEKELHP KTQSVLKEPE PTDTTTYKNL QHHDYNTYTF LDLNLDLSK FRLPQPSSGR ESPRH

+
Macromolecule #45: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 45 / Number of copies: 6 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

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

+
Macromolecule #46: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 46 / Number of copies: 4 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

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

+
Macromolecule #47: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 47 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

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

+
Macromolecule #48: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 48 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

+
Macromolecule #49: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 49 / Number of copies: 9 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

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

+
Macromolecule #50: (3~{S},5~{S})-5-methyl-3-[(13~{R})-13-oxidanyl-13-[(2~{R},5~{R})-...

MacromoleculeName: (3~{S},5~{S})-5-methyl-3-[(13~{R})-13-oxidanyl-13-[(2~{R},5~{R})-5-[(2~{R},5~{R})-5-[(1~{R})-1-oxidanylundecyl]oxolan-2-yl]oxolan-2-yl]tridecyl]oxolan-2-one
type: ligand / ID: 50 / Number of copies: 1 / Formula: 88I
Molecular weightTheoretical: 608.932 Da
Chemical component information

ChemComp-88I:
(3~{S},5~{S})-5-methyl-3-[(13~{R})-13-oxidanyl-13-[(2~{R},5~{R})-5-[(2~{R},5~{R})-5-[(1~{R})-1-oxidanylundecyl]oxolan-2-yl]oxolan-2-yl]tridecyl]oxolan-2-one

+
Macromolecule #51: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 51 / Number of copies: 7 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

+
Macromolecule #52: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 52 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

+
Macromolecule #53: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 53 / 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

+
Macromolecule #54: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 54 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

+
Macromolecule #55: ~{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: 55 / 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

-
Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.55
Component:
ConcentrationName
20.0 mMTris-HClTris
200.0 mMNaClSodium chloride
0.02 w/v (%)n-Dodecyl-B-D-Maltoside

Details: pH 7.55 at 25 degrees Celsius
GridModel: UltrAuFoil R0.6/1 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Support film - Film thickness: 50.0 nm / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR
Details: 20 mA glow discharge. Followed by a 2-day PEGylation with a PEG-thiol reagent.
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK III

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.7 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 130000
Specialist opticsEnergy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 1286 / Average exposure time: 10.0 sec. / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Particle selectionNumber selected: 114209
CTF correctionSoftware - Name: Gctf
Startup modelType of model: EMDB MAP
Details: 60-angstrom low-pass-filtered in-house map from previous work
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 3.1)
Details: Initial 2D classification to remove non-protein particles
Final 3D classificationNumber classes: 2 / Software - Name: RELION (ver. 3.1)
Details: Used a mask classification without alignment on a small region to isolated a compound-bound state.
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Details: RELION solvent-flattened 3D refinement with a PDB-generated mask
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Details: Generated with a mask in RELION / Number images used: 15754
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6zr2

RefinementSpace: REAL
Output model

PDB-7psa:
The acetogenin-bound complex I of Mus musculus resolved to 3.4 angstroms

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