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Open data
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Basic information
| Entry | Database: PDB / ID: 8zno | |||||||||||||||||||||
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| Title | Cryo-EM structure of Arachis hypogaea bc1 complex | |||||||||||||||||||||
Components |
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Keywords | PLANT PROTEIN / Complex / mitochondria / ELECTRON TRANSPORT / MEMBRANE PROTEIN | |||||||||||||||||||||
| Function / homology | Function and homology informationmitochondrial processing peptidase / respiratory chain complex III / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / electron transfer activity / mitochondrial inner membrane / heme binding ...mitochondrial processing peptidase / respiratory chain complex III / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / electron transfer activity / mitochondrial inner membrane / heme binding / mitochondrion / proteolysis / metal ion binding / membrane Similarity search - Function | |||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.02 Å | |||||||||||||||||||||
Authors | Ye, Y. / Dong, J.Q. / Yang, G.F. | |||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: To be PublishedTitle: Cryo-EM structure of Arachis hypogaea bc1 complex Authors: Ye, Y. / Dong, J.Q. / Yang, G.F. | |||||||||||||||||||||
| 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 | 8zno.cif.gz | 770.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8zno.ent.gz | 625.4 KB | Display | PDB format |
| PDBx/mmJSON format | 8zno.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8zno_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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| Full document | 8zno_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 8zno_validation.xml.gz | 102.2 KB | Display | |
| Data in CIF | 8zno_validation.cif.gz | 143.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zn/8zno ftp://data.pdbj.org/pub/pdb/validation_reports/zn/8zno | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 60275MC 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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Links
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Assembly
| Deposited unit | ![]()
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Components
-Mitochondrial-processing peptidase subunit ... , 2 types, 4 molecules AMBN
| #1: Protein | Mass: 49779.320 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 54822.918 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein , 3 types, 6 molecules CODPJV
| #3: Protein | Mass: 43360.520 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 26894.418 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 6867.850 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Cytochrome b-c1 complex subunit ... , 4 types, 8 molecules EQFRGSHT
| #5: Protein | Mass: 21779.992 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: A0A445CTC8, quinol-cytochrome-c reductase #6: Protein | Mass: 14022.236 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 8102.475 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 7448.683 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein/peptide , 1 types, 2 molecules KW
| #10: Protein/peptide | Mass: 3073.544 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 7 types, 30 molecules 












| #11: Chemical | | #12: Chemical | ChemComp-CDL / #13: Chemical | ChemComp-3PE / #14: Chemical | ChemComp-HEM / #15: Chemical | #16: Chemical | #17: Chemical | ChemComp-PC1 / | |
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-Details
| Has ligand of interest | Y |
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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: Arachis hypogaea bc1 complex / Type: COMPLEX / Entity ID: #1-#10 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| 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: 130000 X / Nominal defocus max: 1800 nm / Nominal defocus min: 1600 nm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Electron dose: 48.42 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.02 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 53892 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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FIELD EMISSION GUN