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Open data
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Basic information
| Entry | Database: PDB / ID: 9cwt | |||||||||||||||
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| Title | Human kidney respiratory complex I | |||||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / human / kidney / respiratory complex I | |||||||||||||||
| Function / homology | Function and homology informationprotein lipoylation / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / Respiratory electron transport / protein insertion into mitochondrial inner membrane / ubiquinone biosynthetic process / blastocyst hatching / cellular respiration / cellular response to oxygen levels ...protein lipoylation / Complex I biogenesis / Mitochondrial Fatty Acid Beta-Oxidation / Protein lipoylation / Respiratory electron transport / protein insertion into mitochondrial inner membrane / ubiquinone biosynthetic process / blastocyst hatching / cellular respiration / cellular response to oxygen levels / response to light intensity / mesenchymal stem cell proliferation / Mitochondrial protein import / reproductive system development / iron-sulfur cluster assembly complex / respiratory chain complex / mitochondrial [2Fe-2S] assembly complex / mitochondrial large ribosomal subunit binding / gliogenesis / mesenchymal stem cell differentiation / circulatory system development / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / negative regulation of non-canonical NF-kappaB signal transduction / cardiac muscle tissue development / neural precursor cell proliferation / [2Fe-2S] cluster assembly / oxygen sensor activity / positive regulation of mitochondrial membrane potential / response to hydroperoxide / azurophil granule membrane / cellular response to glucocorticoid stimulus / stem cell division / NADH dehydrogenase activity / iron-sulfur cluster assembly / sodium ion transport / acyl binding / ubiquinone binding / electron transport coupled proton transport / acyl carrier activity / NADH:ubiquinone reductase (H+-translocating) / mitochondrial ATP synthesis coupled electron transport / regulation of protein phosphorylation / positive regulation of ATP biosynthetic process / mitochondrial respiratory chain complex I assembly / mitochondrial electron transport, NADH to ubiquinone / proton motive force-driven mitochondrial ATP synthesis / RHOG GTPase cycle / respiratory chain complex I / response to cAMP / positive regulation of execution phase of apoptosis / NADH dehydrogenase (ubiquinone) activity / endopeptidase activator activity / quinone binding / cellular response to interferon-beta / negative regulation of reactive oxygen species biosynthetic process / extrinsic apoptotic signaling pathway / cellular response to retinoic acid / neurogenesis / ionotropic glutamate receptor binding / Mitochondrial protein degradation / substantia nigra development / muscle contraction / reactive oxygen species metabolic process / aerobic respiration / synaptic membrane / cerebellum development / fatty acid binding / regulation of mitochondrial membrane potential / respiratory electron transport chain / response to nicotine / DNA damage response, signal transduction by p53 class mediator / kidney development / response to hydrogen peroxide / monooxygenase activity / sensory perception of sound / fatty acid metabolic process / circadian rhythm / brain development / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / multicellular organism growth / NAD binding / positive regulation of protein catabolic process / fatty acid biosynthetic process / cellular senescence / FMN binding / nervous system development / 4 iron, 4 sulfur cluster binding / response to oxidative stress / protease binding / response to ethanol / gene expression / in utero embryonic development / response to hypoxia / electron transfer activity / mitochondrial inner membrane / nuclear speck / nuclear body / mitochondrial matrix Similarity search - Function | |||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.44 Å | |||||||||||||||
Authors | Zhang, Z. / Lyu, M. | |||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: Human kidney respiratory complex I Authors: Zhang, Z. / Lyu, M. | |||||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9cwt.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9cwt.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 9cwt.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9cwt_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 9cwt_full_validation.pdf.gz | 1.6 MB | Display | |
| Data in XML | 9cwt_validation.xml.gz | 187.5 KB | Display | |
| Data in CIF | 9cwt_validation.cif.gz | 303 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cw/9cwt ftp://data.pdbj.org/pub/pdb/validation_reports/cw/9cwt | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 45974MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Assembly
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Components
-NADH dehydrogenase [ubiquinone] flavoprotein ... , 3 types, 3 molecules AKO
| #1: Protein | Mass: 50886.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P49821, NADH:ubiquinone reductase (H+-translocating) |
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| #10: Protein | Mass: 11958.526 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P56181 |
| #14: Protein | Mass: 27425.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P19404, NADH:ubiquinone reductase (H+-translocating) |
-NADH dehydrogenase [ubiquinone] iron-sulfur protein ... , 7 types, 7 molecules BCLPQTh
| #2: Protein | Mass: 23734.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: O00217, NADH:ubiquinone reductase (H+-translocating) |
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| #3: Protein | Mass: 23595.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: O75251, NADH:ubiquinone reductase (H+-translocating) |
| #11: Protein | Mass: 20139.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43181 |
| #15: Protein | Mass: 30281.490 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: O75489, NADH:ubiquinone reductase (H+-translocating) |
| #16: Protein | Mass: 52613.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: O75306, NADH:ubiquinone reductase (H+-translocating) |
| #18: Protein | Mass: 13733.654 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75380 |
| #31: Protein | Mass: 12542.563 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43920 |
-NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit ... , 11 types, 11 molecules EFHIJNSUVWu
| #4: Protein | Mass: 15165.603 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P56556 |
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| #5: Protein | Mass: 10937.563 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43678 |
| #7: Protein | Mass: 13477.665 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16718 |
| #8: Protein | Mass: 12571.403 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95182 |
| #9: Protein | Mass: 42575.527 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16795 |
| #13: Protein | Mass: 17140.445 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UI09 |
| #17: Protein | Mass: 8084.391 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O15239 |
| #19: Protein | Mass: 9287.797 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95167 |
| #20: Protein | Mass: 14868.050 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q86Y39 |
| #21: Protein | Mass: 16721.311 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9P0J0 |
| #41: Protein | Mass: 20139.100 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P51970 |
-Protein , 2 types, 3 molecules GXM
| #6: Protein | Mass: 17434.273 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O14561#12: Protein | | Mass: 79557.383 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P28331, NADH:ubiquinone reductase (H+-translocating) |
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-NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit ... , 11 types, 11 molecules YZabcdenopv
| #22: Protein | Mass: 12072.403 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95178 |
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| #23: Protein | Mass: 11425.006 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43676 |
| #24: Protein | Mass: 21784.285 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43674 |
| #25: Protein | Mass: 15517.228 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95139 |
| #26: Protein | Mass: 21791.744 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95169 |
| #27: Protein | Mass: 20808.729 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O96000 |
| #28: Protein | Mass: 17336.617 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NX14 |
| #36: Protein | Mass: 6972.210 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75438 |
| #37: Protein | Mass: 15231.596 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95168 |
| #38: Protein | Mass: 21866.955 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y6M9 |
| #42: Protein | Mass: 16435.045 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P17568 |
-NADH dehydrogenase [ubiquinone] 1 subunit ... , 2 types, 2 molecules fg
| #29: Protein | Mass: 8747.248 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43677 |
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| #30: Protein | Mass: 14209.521 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95298 |
-NADH-ubiquinone oxidoreductase chain ... , 7 types, 7 molecules jklmrsi
| #32: Protein | Mass: 13189.951 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03897, NADH:ubiquinone reductase (H+-translocating) |
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| #33: Protein | Mass: 10745.110 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03901, NADH:ubiquinone reductase (H+-translocating) |
| #34: Protein | Mass: 67068.930 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03915, NADH:ubiquinone reductase (H+-translocating) |
| #35: Protein | Mass: 18626.963 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03923, NADH:ubiquinone reductase (H+-translocating) |
| #39: Protein | Mass: 51613.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03905, NADH:ubiquinone reductase (H+-translocating) |
| #40: Protein | Mass: 35676.266 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03886, NADH:ubiquinone reductase (H+-translocating) |
| #44: Protein | Mass: 38980.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P03891, NADH:ubiquinone reductase (H+-translocating) |
-Protein/peptide , 1 types, 1 molecules D
| #43: Protein/peptide | Mass: 1890.321 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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-Non-polymers , 5 types, 11 molecules 








| #45: Chemical | ChemComp-SF4 / #46: Chemical | ChemComp-FMN / | #47: Chemical | ChemComp-ZMP / | #48: Chemical | ChemComp-NDP / | #49: Chemical | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: respiratory complex I / Type: COMPLEX / Entity ID: #1-#44 / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 1500 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 38 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 3.44 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 16097 / Symmetry type: POINT |
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Homo sapiens (human)
United States, 1items
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