Research workbench
Crystal structure of bovine mitochondrial cytochrome BC1 complex, alpha carbon atoms only
Analyse Crystal structure of bovine mitochondrial cytochrome BC1 complex, alpha carbon… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QCR
- Type
- protein
- Length
- 1,883 residues
- Chains
- 11
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquinol cytochrome C oxidoreductase
- EC
- 1.10.2.2
- UniProt
- P31800, P23004, P00157, P00125, P13272, P00129, P13271, P00126, P00130, P07552
- Ligands
- HEM
- Pockets
- 4 · best druggability 0.38
Structure
x-ray diffraction · 11 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 446 | 0% helix, 0% strand | P31800 |
| B | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 423 | 0% helix, 0% strand | P23004 |
| C | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 378 | 0% helix, 0% strand | P00157 |
| D | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 75 | 0% helix, 0% strand | P00125 |
| E | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 196 | 0% helix, 0% strand | P13272 |
| F | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 103 | 0% helix, 0% strand | P00129 |
| G | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 70 | 0% helix, 0% strand | P13271 |
| H | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 60 | 0% helix, 0% strand | P00126 |
| I | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 28 | 0% helix, 0% strand | P13272 |
| J | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 59 | 0% helix, 0% strand | P00130 |
| K | Ubiquinol cytochrome C oxidoreductase (EC 1.10.2.2) | protein | 45 | 0% helix, 0% strand | P07552 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.38 | 0.73 | 26 | empty |
| 2 | 69 | 0.32 | 0.73 | 24 | empty |
| 3 | 66 | 0.31 | 0.73 | 28 | empty |
| 4 | 53 | 0.28 | 0.72 | 18 | empty |
Interfaces
15 interfaces between chains.
- A–B · 276 Ų buried · 0 hydrogen bonds · protein-protein
- A–G · 185 Ų buried · 0 hydrogen bonds · protein-protein
- D–G · 167 Ų buried · 0 hydrogen bonds · protein-protein
- C–F · 137 Ų buried · 0 hydrogen bonds · protein-protein
- A–E · 125 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1QCR · Crystal structure of bovine mitochondrial cytochrome BC1 complex, alpha carbon atoms only · the same entry in another collection · chain J against J, TM-score 1.00
- P31800 · AlphaFold monomer V2.0 prediction for cytochrome B-C1 complex subunit 1, mitochondrial… · a predicted model of the same protein · chain A against A, TM-score 0.98
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
- Every structure of UniProt P07552
- Elsewhere: RCSB PDB 1QCR · PDBe 1QCR · UniProt P31800 · UniProt P23004 · UniProt P00157 · UniProt P00125 · UniProt P13272 · UniProt P00129 · UniProt P13271 · UniProt P00126 · UniProt P00130 · UniProt P07552
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