Research workbench
AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (C3MQL5)
Analyse AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (C3MQL5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3MQL5
- Type
- protein
- Length
- 592 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9d37280c8D61e058C5085fA10417ECaD4341F28c
- Molecule
- V-type ATP synthase alpha chain
- UniProt
- C3MQL5
- Pockets
- 5 · best druggability 0.56
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 | C3MQL5 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.56 | 0.80 | 22 | empty |
| 2 | 173 | 0.51 | 0.78 | 33 | empty |
| 3 | 58 | 0.42 | 0.82 | 18 | empty |
| 4 | 54 | 0.32 | 0.77 | 14 | empty |
| 5 | 60 | 0.30 | 0.74 | 17 | 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 C3MQL5
- Elsewhere: UniProt C3MQL5 · AlphaFold DB C3MQL5
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