Research workbench
AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (A4FXD4)
Analyse AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (A4FXD4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4FXD4
- Type
- protein
- Length
- 586 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9b6C8748fA09344FB129a858B9697b80Fa910902
- Molecule
- V-type ATP synthase alpha chain
- UniProt
- A4FXD4
- Pockets
- 8 · best druggability 0.55
Structure
1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase alpha chain | protein | 586 | 37% helix, 25% strand | A4FXD4 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.55 | 0.78 | 21 | empty |
| 2 | 190 | 0.52 | 0.77 | 27 | empty |
| 3 | 63 | 0.41 | 0.81 | 14 | empty |
| 4 | 68 | 0.39 | 0.79 | 17 | empty |
| 5 | 81 | 0.38 | 0.77 | 18 | empty |
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 A4FXD4
- Elsewhere: UniProt A4FXD4 · AlphaFold DB A4FXD4
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