Research workbench
AlphaFold monomer V2.0 prediction for V-type proton ATPase catalytic subunit a (Q29048)
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
- Q29048
- Type
- protein
- Length
- 617 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xFb1Fd01bBa777F5321d3CeBE17CEDAC28290Fb4D
- Molecule
- V-type proton ATPase catalytic subunit a
- UniProt
- Q29048
- Pockets
- 9 · best druggability 0.53
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 | Q29048 |
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.53 | 0.77 | 35 | empty |
| 2 | 72 | 0.44 | 0.81 | 20 | empty |
| 3 | 60 | 0.44 | 0.82 | 14 | empty |
| 4 | 156 | 0.42 | 0.74 | 25 | empty |
| 5 | 152 | 0.42 | 0.74 | 28 | empty |
Compared structures
- 7U8P · Structure of porcine kidney V-ATPase with SidK, Rotary State 1 · an experimental structure of the same protein · chain A against C, TM-score 0.96
- 7U8R · Structure of porcine kidney V-ATPase with SidK, Rotary State 3 · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 7U8Q · Structure of porcine kidney V-ATPase with SidK, Rotary State 2 · an experimental structure of the same protein · chain A against B, TM-score 0.96
- 7U8O · Structure of porcine V-ATPase with mEAK7 and SidK, Rotary state 2 · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 Q29048
- Elsewhere: UniProt Q29048 · AlphaFold DB Q29048
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