Research workbench
AlphaFold monomer V2.0 prediction for bacillolysin (P23384)
Analyse AlphaFold monomer V2.0 prediction for bacillolysin (P23384) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23384
- Type
- protein
- Length
- 544 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2E70618e0388072122786Fd80c7EC6179fE5f698
- Molecule
- Bacillolysin
- UniProt
- P23384
- Pockets
- 6 · best druggability 0.63
Structure
1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bacillolysin | protein | 544 | 30% helix, 27% strand | P23384 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 364 | 0.63 | 0.78 | 37 | empty |
| 2 | 273 | 0.61 | 0.80 | 30 | empty |
| 3 | 187 | 0.57 | 0.81 | 33 | empty |
| 4 | 77 | 0.33 | 0.75 | 14 | empty |
| 5 | 76 | 0.32 | 0.74 | 20 | 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 P23384
- Elsewhere: UniProt P23384 · AlphaFold DB P23384
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