Research workbench
AlphaFold monomer V2.0 prediction for V-type proton ATPase catalytic subunit a (P49087)
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
- P49087
- Type
- protein
- Length
- 561 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x638EA7d798aBF8bbDfE1dCA65BB71AD6E3a92db9
- Molecule
- V-type proton ATPase catalytic subunit a
- UniProt
- P49087
- Pockets
- 8 · best druggability 0.48
Structure
1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type proton ATPase catalytic subunit a | protein | 561 | 42% helix, 21% strand | P49087 |
Pockets
8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.48 | 0.76 | 32 | empty |
| 2 | 224 | 0.45 | 0.73 | 28 | empty |
| 3 | 76 | 0.40 | 0.79 | 19 | empty |
| 4 | 145 | 0.39 | 0.73 | 20 | empty |
| 5 | 83 | 0.37 | 0.77 | 14 | 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 P49087
- Elsewhere: UniProt P49087 · AlphaFold DB P49087
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