Research workbench
AlphaFold monomer V2.0 prediction for V-type proton ATPase catalytic subunit a (Q5R5H2)
Analyse AlphaFold monomer V2.0 prediction for V-type proton ATPase catalytic subunit a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5R5H2
- Type
- protein
- Length
- 617 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc87019A1CC09AD435548CEeAeAc61B1e4Ca83541
- Molecule
- V-type proton ATPase catalytic subunit a
- UniProt
- Q5R5H2
- Pockets
- 10 · best druggability 0.50
Structure
1 distinct chain · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type proton ATPase catalytic subunit a | protein | 617 | 39% helix, 25% strand | Q5R5H2 |
Pockets
10 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.50 | 0.77 | 30 | empty |
| 2 | 79 | 0.43 | 0.80 | 23 | empty |
| 3 | 163 | 0.43 | 0.74 | 29 | empty |
| 4 | 57 | 0.42 | 0.82 | 14 | empty |
| 5 | 143 | 0.41 | 0.74 | 18 | 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 Q5R5H2
- Elsewhere: UniProt Q5R5H2 · AlphaFold DB Q5R5H2
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