Research workbench
AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (A3DHP0)
Analyse AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (A3DHP0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3DHP0
- Type
- protein
- Length
- 589 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x844c0a881E7457F55a632E14DcEd1163DE274C59
- Molecule
- V-type ATP synthase alpha chain
- UniProt
- A3DHP0
- Pockets
- 6 · best druggability 0.58
Structure
1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase alpha chain | protein | 589 | 38% helix, 24% strand | A3DHP0 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.58 | 0.80 | 21 | empty |
| 2 | 204 | 0.53 | 0.77 | 33 | empty |
| 3 | 59 | 0.44 | 0.83 | 13 | empty |
| 4 | 94 | 0.37 | 0.76 | 16 | empty |
| 5 | 83 | 0.37 | 0.76 | 16 | 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 A3DHP0
- Elsewhere: UniProt A3DHP0 · AlphaFold DB A3DHP0
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