Research workbench
AlphaFold monomer V2.0 prediction for phospholipase A1-II 1 (A2WT95)
Analyse AlphaFold monomer V2.0 prediction for phospholipase A1-II 1 (A2WT95) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2WT95
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
- Molecule
- Phospholipase A1-II 1
- UniProt
- A2WT95
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase A1-II 1 | protein | 393 | 32% helix, 19% strand | A2WT95 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.64 | 0.91 | 17 | empty |
| 2 | 208 | 0.55 | 0.78 | 26 | empty |
| 3 | 96 | 0.44 | 0.79 | 21 | empty |
| 4 | 96 | 0.36 | 0.75 | 19 | 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 A2WT95
- Elsewhere: UniProt A2WT95 · AlphaFold DB A2WT95
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