Research workbench
AlphaFold monomer V2.0 prediction for V-type proton ATPase catalytic subunit a (O16109)
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
- O16109
- Type
- protein
- Length
- 614 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7B7AB9CFf896c6Dfc7d6EbD15e1E38bb0c14f53B
- Molecule
- V-type proton ATPase catalytic subunit a
- UniProt
- O16109
- Pockets
- 10 · best druggability 0.66
Structure
1 distinct chain · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type proton ATPase catalytic subunit a | protein | 614 | 39% helix, 26% strand | O16109 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.66 | 0.81 | 41 | empty |
| 2 | 188 | 0.53 | 0.78 | 30 | empty |
| 3 | 183 | 0.46 | 0.75 | 30 | empty |
| 4 | 61 | 0.45 | 0.83 | 13 | empty |
| 5 | 60 | 0.36 | 0.79 | 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 O16109
- Elsewhere: UniProt O16109 · AlphaFold DB O16109
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