Research workbench
AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit C 1 (Q4R5H9)
Analyse AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit C 1 (Q4R5H9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4R5H9
- Type
- protein
- Length
- 382 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- V-type proton ATPase subunit C 1
- UniProt
- Q4R5H9
- Pockets
- 4 · best druggability 0.61
Structure
1 distinct chain · 56% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type proton ATPase subunit C 1 | protein | 382 | 56% helix, 15% strand | Q4R5H9 |
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 | 490 | 0.61 | 0.75 | 37 | empty |
| 2 | 81 | 0.43 | 0.80 | 15 | empty |
| 3 | 53 | 0.31 | 0.76 | 12 | empty |
| 4 | 59 | 0.30 | 0.75 | 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 Q4R5H9
- Elsewhere: UniProt Q4R5H9 · AlphaFold DB Q4R5H9
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