MolNFT v1 · #149032 · protein
Cryoem structure of bovine cytochrome BC1 with no ligand bound
6FO2 · Cytochrome B-C1 complex subunit 1, mitochondrial: “Cryoem structure of bovine cytochrome BC1 with no ligand bound”. Electron microscopy, 2 ligands (HEM, HEC), 20 pockets (best druggability 0.85). MolNFT v1 #149032 on GenesisL1: 3D…
- PDB
- 6FO2
- Type
- protein
- Length
- 3,865 residues
- Chains
- 20
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome B-C1 complex subunit 1, mitochondrial; Cytochrome B-C1 complex subunit 2…
- EC
- 1.10.2.2
- UniProt
- P31800, P23004, P00157, P00125, P13272, P00129, P13271, P00126, P00130
- Ligands
- HEM, HEC
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 12 distinct chains · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| N, A | Cytochrome B-C1 complex subunit 1, mitochondrial | protein | 438 | 45% helix, 18% strand | P31800 |
| O | Cytochrome B-C1 complex subunit 2, mitochondrial | protein | 411 | 41% helix, 19% strand | P23004 |
| P, C | Cytochrome B | protein | 370 | 69% helix, 1% strand | P00157 |
| Q, D | Cytochrome C1, heme protein, mitochondrial | protein | 237 | 39% helix, 9% strand | P00125 |
| R | Cytochrome B-C1 complex subunit rieske, mitochondrial (EC 1.10.2.2) | protein | 168 | 29% helix, 12% strand | P13272 |
| S, F | Cytochrome B-C1 complex subunit 7 | protein | 98 | 61% helix, 0% strand | P00129 |
| T, G | Cytochrome B-C1 complex subunit 8 | protein | 74 | 53% helix, 9% strand | P13271 |
| U, H | Cytochrome B-C1 complex subunit 6, mitochondrial | protein | 65 | 75% helix, 0% strand | P00126 |
| V, I | Cytochrome B-C1 complex subunit rieske, mitochondrial (EC 1.10.2.2) | protein | 16 | 0% helix, 38% strand | P13272 |
| W, J | Cytochrome B-C1 complex subunit 9 | protein | 56 | 77% helix, 0% strand | P00130 |
| B | Cytochrome B-C1 complex subunit 2, mitochondrial | protein | 409 | 42% helix, 19% strand | P23004 |
| E | Cytochrome B-C1 complex subunit rieske, mitochondrial (EC 1.10.2.2) | protein | 169 | 28% helix, 12% strand | P13272 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains P, C
- HEC · Heme C · ligand · 2 copies · chains Q, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 396 | 0.85 | 0.93 | 44 | HEM |
| 2 | 815 | 0.85 | 0.87 | 76 | HEM |
| 3 | 403 | 0.84 | 0.92 | 47 | HEM |
| 4 | 1116 | 0.83 | 0.84 | 127 | HEC |
| 5 | 214 | 0.83 | 0.96 | 30 | empty |
Interfaces
55 interfaces between chains.
- N–O · 2130 Ų buried · 39 hydrogen bonds · protein-protein
- A–B · 2122 Ų buried · 36 hydrogen bonds · protein-protein
- P–Q · 1751 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1743 Ų buried · 16 hydrogen bonds · protein-protein
- P–C · 1236 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6FO2 · CryoEM structure of bovine cytochrome bc1 with no ligand bound · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P31800
- Every structure of UniProt P23004
- Every structure of UniProt P00157
- Every structure of UniProt P00125
- Every structure of UniProt P13272
- Every structure of UniProt P00129
- Every structure of UniProt P13271
- Every structure of UniProt P00126
- Every structure of UniProt P00130
- Elsewhere: RCSB PDB 6FO2 · PDBe 6FO2 · UniProt P31800 · UniProt P23004 · UniProt P00157 · UniProt P00125 · UniProt P13272 · UniProt P00129 · UniProt P13271 · UniProt P00126 · UniProt P00130
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