Research workbench
AlphaFold monomer V2.0 prediction for beta-xylosidase (O30360)
Analyse AlphaFold monomer V2.0 prediction for beta-xylosidase (O30360) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O30360
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Beta-xylosidase
- UniProt
- O30360
- Pockets
- 4 · best druggability 0.55
Structure
1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-xylosidase | protein | 500 | 32% helix, 27% strand | O30360 |
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 | 227 | 0.55 | 0.78 | 30 | empty |
| 2 | 93 | 0.50 | 0.83 | 30 | empty |
| 3 | 103 | 0.35 | 0.73 | 17 | empty |
| 4 | 61 | 0.30 | 0.74 | 18 | 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 O30360
- Elsewhere: UniProt O30360 · AlphaFold DB O30360
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