Research workbench
Cytochrome BC1 complex from bovine
Analyse Cytochrome BC1 complex from bovine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BE3
- Type
- protein
- Length
- 2,049 residues
- Chains
- 11
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome BC1 complex
- EC
- 1.10.2.2
- UniProt
- P31800, P23004, P00157, P00125, P13272, P00129, P13271, P00126, P00130, P07552
- Ligands
- HEM, HEC, FES
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 11 distinct chains · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 446 | 45% helix, 16% strand | P31800 |
| B | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 419 | 45% helix, 17% strand | P23004 |
| C | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 379 | 69% helix, 2% strand | P00157 |
| D | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 241 | 42% helix, 2% strand | P00125 |
| E | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 196 | 31% helix, 17% strand | P13272 |
| F | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 106 | 67% helix, 0% strand | P00129 |
| G | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 81 | 53% helix, 11% strand | P13271 |
| H | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 64 | 73% helix, 0% strand | P00126 |
| I | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 33 | 0% helix, 21% strand | P13272 |
| J | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 62 | 71% helix, 0% strand | P00130 |
| K | Cytochrome BC1 complex (EC 1.10.2.2) | protein | 22 | 86% helix, 0% strand | P07552 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains C
- HEC · Heme C · ligand · chains D
- FES · Fe2/s2 (inorganic) cluster · ligand · chains E
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 | 550 | 0.87 | 0.93 | 62 | HEM |
| 2 | 1130 | 0.84 | 0.84 | 110 | empty |
| 3 | 1199 | 0.79 | 0.80 | 100 | empty |
| 4 | 521 | 0.79 | 0.85 | 54 | HEM |
| 5 | 1118 | 0.77 | 0.79 | 118 | empty |
Interfaces
25 interfaces between chains.
- A–B · 2068 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 1647 Ų buried · 16 hydrogen bonds · protein-protein
- B–I · 1553 Ų buried · 14 hydrogen bonds · protein-protein
- C–F · 1224 Ų buried · 11 hydrogen bonds · protein-protein
- D–H · 1174 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 2 cofactor (disulfide, heme c attachment).
Compared structures
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 1BE3 · PDBe 1BE3 · UniProt P31800 · UniProt P23004 · UniProt P00157 · UniProt P00125 · UniProt P13272 · UniProt P00129 · UniProt P13271 · UniProt P00126 · UniProt P00130 · UniProt P07552
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