Research workbench
E. COLI ATP synthase ADP sub-state 3A fo focussed
Analyse E. COLI ATP synthase ADP sub-state 3A fo focussed in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VWK
- Type
- protein
- Length
- 1,133 residues
- Chains
- 13
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase subunit C; ATP synthase subunit B; ATP synthase subunit a
- UniProt
- F4TL55, D6IFY0, C3SL77
- Pockets
- 11 · best druggability 0.74
Structure
electron microscopy · 4 distinct chains · 80% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| I, J, L, M, N, O, P, Q, R, S | ATP synthase subunit C | protein | 77 | 96% helix, 0% strand | F4TL55 |
| X | ATP synthase subunit B | protein | 47 | 85% helix, 0% strand | D6IFY0 |
| Y | ATP synthase subunit B | protein | 50 | 94% helix, 0% strand | D6IFY0 |
| a | ATP synthase subunit a | protein | 266 | 72% helix, 3% strand | C3SL77 |
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 464 | 0.74 | 0.83 | 52 | empty |
| 2 | 896 | 0.70 | 0.74 | 78 | empty |
| 3 | 59 | 0.70 | 0.97 | 27 | empty |
| 4 | 779 | 0.69 | 0.75 | 67 | empty |
| 5 | 145 | 0.58 | 0.83 | 18 | empty |
Interfaces
18 interfaces between chains.
- X–a · 1752 Ų buried · 20 hydrogen bonds · protein-protein
- R–S · 1662 Ų buried · 2 hydrogen bonds · protein-protein
- N–S · 1648 Ų buried · 2 hydrogen bonds · protein-protein
- I–Q · 1637 Ų buried · 2 hydrogen bonds · protein-protein
- I–P · 1632 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6VWK · E. coli ATP Synthase ADP Sub-state 3a Fo Focussed · the same entry in another collection · chain I against I, 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 F4TL55
- Every structure of UniProt D6IFY0
- Every structure of UniProt C3SL77
- Elsewhere: RCSB PDB 6VWK · PDBe 6VWK · UniProt F4TL55 · UniProt D6IFY0 · UniProt C3SL77
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