Research workbench
Bovine ATP synthase rotor domain, state 1
Analyse Bovine ATP synthase rotor domain, state 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZG7
- Type
- protein
- Length
- 1,048 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase subunit gamma, mitochondrial; ATP synthase subunit delta, mitochondrial; ATP…
- UniProt
- P05631, P05630, P05632, P07926
- Pockets
- 10 · best druggability 0.84
Structure
electron microscopy · 5 distinct chains · 61% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G | ATP synthase subunit gamma, mitochondrial | protein | 272 | 62% helix, 13% strand | P05631 |
| H | ATP synthase subunit delta, mitochondrial | protein | 132 | 30% helix, 38% strand | P05630 |
| I | ATP synthase subunit epsilon, mitochondrial | protein | 47 | 55% helix, 9% strand | P05632 |
| R, M, N, Q, O | ATP synthase F(0) complex subunit C2, mitochondrial | protein | 75 | 88% helix, 0% strand | P07926 |
| K, L, P | ATP synthase F(0) complex subunit C2, mitochondrial | protein | 74 | 91% helix, 0% strand | P07926 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.84 | 0.91 | 54 | empty |
| 2 | 401 | 0.83 | 0.92 | 47 | empty |
| 3 | 608 | 0.75 | 0.81 | 56 | empty |
| 4 | 161 | 0.58 | 0.82 | 21 | empty |
| 5 | 135 | 0.55 | 0.82 | 26 | empty |
Interfaces
26 interfaces between chains.
- M–N · 1617 Ų buried · 8 hydrogen bonds · protein-protein
- R–Q · 1606 Ų buried · 11 hydrogen bonds · protein-protein
- L–M · 1602 Ų buried · 9 hydrogen bonds · protein-protein
- N–O · 1548 Ų buried · 6 hydrogen bonds · protein-protein
- P–Q · 1547 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (methylation).
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 P05631
- Every structure of UniProt P05630
- Every structure of UniProt P05632
- Every structure of UniProt P07926
- Elsewhere: RCSB PDB 6ZG7 · PDBe 6ZG7 · UniProt P05631 · UniProt P05630 · UniProt P05632 · UniProt P07926
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