Research workbench
AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (Q5XE50)
Analyse AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (Q5XE50) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5XE50
- Type
- protein
- Length
- 591 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- V-type ATP synthase alpha chain
- UniProt
- Q5XE50
- Pockets
- 9 · best druggability 0.55
Structure
1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase alpha chain | protein | 591 | 38% helix, 24% strand | Q5XE50 |
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.55 | 0.80 | 23 | empty |
| 2 | 198 | 0.50 | 0.76 | 32 | empty |
| 3 | 50 | 0.46 | 0.85 | 18 | empty |
| 4 | 91 | 0.45 | 0.80 | 16 | empty |
| 5 | 78 | 0.44 | 0.80 | 20 | 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 Q5XE50
- Elsewhere: UniProt Q5XE50 · AlphaFold DB Q5XE50
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