Research workbench
AlphaFold monomer V2.0 prediction for phospholipase a-2-activating protein (P27612)
Analyse AlphaFold monomer V2.0 prediction for phospholipase a-2-activating protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27612
- Type
- protein
- Length
- 794 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Phospholipase a-2-activating protein
- UniProt
- P27612
- Pockets
- 7 · best druggability 0.77
Structure
1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase a-2-activating protein | protein | 794 | 30% helix, 26% strand | P27612 |
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 691 | 0.77 | 0.82 | 58 | empty |
| 2 | 735 | 0.73 | 0.79 | 67 | empty |
| 3 | 158 | 0.73 | 0.91 | 22 | empty |
| 4 | 610 | 0.67 | 0.76 | 63 | empty |
| 5 | 153 | 0.51 | 0.79 | 21 | 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 P27612
- Elsewhere: UniProt P27612 · AlphaFold DB P27612
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