Research workbench
AlphaFold monomer V2.0 prediction for phospholipase B (F8S101)
Analyse AlphaFold monomer V2.0 prediction for phospholipase B (F8S101) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F8S101
- Type
- protein
- Length
- 553 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Phospholipase B
- UniProt
- F8S101
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase B | protein | 553 | 36% helix, 23% strand | F8S101 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 853 | 0.80 | 0.83 | 77 | empty |
| 2 | 62 | 0.33 | 0.77 | 12 | empty |
| 3 | 61 | 0.30 | 0.74 | 14 | empty |
| 4 | 50 | 0.26 | 0.73 | 12 | empty |
Modifications
Observed in the structure: 2 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 F8S101
- Elsewhere: UniProt F8S101 · AlphaFold DB F8S101
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