Research workbench
AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit H (Q9LX65)
Analyse AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit H (Q9LX65) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9LX65
- Type
- protein
- Length
- 441 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4F68597e66577F2Fc83E62a655Df07e7Ca4F542e
- Molecule
- V-type proton ATPase subunit H
- UniProt
- Q9LX65
- Pockets
- 4 · best druggability 0.46
Structure
1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type proton ATPase subunit H | protein | 441 | 74% helix, 0% strand | Q9LX65 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.46 | 0.78 | 18 | empty |
| 2 | 62 | 0.30 | 0.75 | 15 | empty |
| 3 | 51 | 0.27 | 0.74 | 12 | empty |
| 4 | 56 | 0.27 | 0.73 | 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 Q9LX65
- Elsewhere: UniProt Q9LX65 · AlphaFold DB Q9LX65
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