Research workbench
Complex of GAMMA/EPSILON ATP synthase from E.COLI
Analyse Complex of GAMMA/EPSILON ATP synthase from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FS0
- Type
- protein
- Length
- 347 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase epsilon subunit; ATP synthase gamma subunit
- EC
- 3.6.1.34
- UniProt
- P0A6E6, P0ABA6
- Pockets
- 6 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | ATP synthase epsilon subunit (EC 3.6.1.34) | protein | 128 | 27% helix, 41% strand | P0A6E6 |
| G | ATP synthase gamma subunit (EC 3.6.1.34) | protein | 219 | 55% helix, 19% strand | P0ABA6 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.45 | 0.76 | 34 | empty |
| 2 | 134 | 0.45 | 0.76 | 18 | empty |
| 3 | 102 | 0.41 | 0.77 | 17 | empty |
| 4 | 56 | 0.37 | 0.79 | 12 | empty |
| 5 | 61 | 0.33 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- E–G · 2156 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 1FS0 · Complex of GAMMA/EPSILON ATP synthase from E.COLI · the same entry in another collection · chain E against E, TM-score 1.00
- P0ABA6 · AlphaFold monomer V2.0 prediction for ATP synthase gamma chain (P0ABA6) · a predicted model of the same protein · chain G against A, TM-score 0.95
- P0A6E6 · AlphaFold monomer V2.0 prediction for ATP synthase epsilon chain (P0A6E6) · a predicted model of the same protein · chain E against A, TM-score 0.63
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 P0A6E6
- Every structure of UniProt P0ABA6
- Elsewhere: RCSB PDB 1FS0 · PDBe 1FS0 · UniProt P0A6E6 · UniProt P0ABA6
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