Research workbench
AlphaFold monomer V2.0 prediction for phospholipase a and acyltransferase 5 (Q9CPX5)
Analyse AlphaFold monomer V2.0 prediction for phospholipase a and acyltransferase 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9CPX5
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Phospholipase a and acyltransferase 5
- UniProt
- Q9CPX5
- Pockets
- 1 · best druggability 0.30
Structure
1 distinct chain · 17% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase a and acyltransferase 5 | protein | 270 | 17% helix, 12% strand | Q9CPX5 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.30 | 0.76 | 15 | 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 Q9CPX5
- Elsewhere: UniProt Q9CPX5 · AlphaFold DB Q9CPX5
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