Research workbench
AlphaFold monomer V2.0 prediction for ATPase H(+)-transporting accessory protein 2 (Q9VHG4)
Analyse AlphaFold monomer V2.0 prediction for ATPase H(+)-transporting accessory… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9VHG4
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA340bF1534bceeae44fe12C7C9F6CF023b79E47e
- Molecule
- ATPase H(+)-transporting accessory protein 2
- UniProt
- Q9VHG4
- Pockets
- 3 · best druggability 0.41
Structure
1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATPase H(+)-transporting accessory protein 2 | protein | 320 | 43% helix, 15% strand | Q9VHG4 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.41 | 0.78 | 18 | empty |
| 2 | 63 | 0.32 | 0.76 | 19 | empty |
| 3 | 51 | 0.24 | 0.72 | 14 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q9VHG4
- Elsewhere: UniProt Q9VHG4 · AlphaFold DB Q9VHG4
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