Research workbench
AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (A7HDG9)
Analyse AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (A7HDG9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7HDG9
- Type
- protein
- Length
- 578 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- V-type ATP synthase alpha chain
- UniProt
- A7HDG9
- Pockets
- 10 · best druggability 0.57
Structure
1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase alpha chain | protein | 578 | 37% helix, 24% strand | A7HDG9 |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 170 | 0.57 | 0.81 | 21 | empty |
| 2 | 50 | 0.56 | 0.90 | 21 | empty |
| 3 | 149 | 0.53 | 0.81 | 22 | empty |
| 4 | 104 | 0.46 | 0.80 | 26 | empty |
| 5 | 141 | 0.44 | 0.76 | 24 | 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 A7HDG9
- Elsewhere: UniProt A7HDG9 · AlphaFold DB A7HDG9
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