Research workbench
AlphaFold monomer V2.0 prediction for phospholipase A1 (P0DSI2)
Analyse AlphaFold monomer V2.0 prediction for phospholipase A1 (P0DSI2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DSI2
- Type
- protein
- Length
- 379 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- Phospholipase A1
- UniProt
- P0DSI2
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase A1 | protein | 379 | 41% helix, 16% strand | P0DSI2 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 943 | 0.75 | 0.78 | 82 | empty |
| 2 | 57 | 0.36 | 0.78 | 16 | empty |
| 3 | 61 | 0.33 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
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 P0DSI2
- Elsewhere: UniProt P0DSI2 · AlphaFold DB P0DSI2
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