Research workbench
AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (A9A2R0)
Analyse AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (A9A2R0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9A2R0
- Type
- protein
- Length
- 592 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7873A5D824374e6d396229A08164bC7953c733b0
- Molecule
- V-type ATP synthase alpha chain
- UniProt
- A9A2R0
- Pockets
- 4 · 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 | 592 | 37% helix, 25% strand | A9A2R0 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.55 | 0.79 | 24 | empty |
| 2 | 165 | 0.47 | 0.76 | 28 | empty |
| 3 | 130 | 0.45 | 0.77 | 30 | empty |
| 4 | 67 | 0.44 | 0.82 | 14 | 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 A9A2R0
- Elsewhere: UniProt A9A2R0 · AlphaFold DB A9A2R0
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