Research workbench
AlphaFold monomer V2.0 prediction for beta-xylosidase (P45704)
Analyse AlphaFold monomer V2.0 prediction for beta-xylosidase (P45704) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P45704
- Type
- protein
- Length
- 618 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0a8CCfe42e026980760C0B967bbe59a752A3A2Fc
- Molecule
- Beta-xylosidase
- UniProt
- P45704
- Pockets
- 10 · best druggability 0.67
Structure
1 distinct chain · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-xylosidase | protein | 618 | 31% helix, 21% strand | P45704 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 371 | 0.67 | 0.81 | 31 | empty |
| 2 | 375 | 0.61 | 0.77 | 30 | empty |
| 3 | 220 | 0.59 | 0.80 | 38 | empty |
| 4 | 233 | 0.50 | 0.75 | 30 | empty |
| 5 | 159 | 0.48 | 0.77 | 30 | 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 P45704
- Elsewhere: UniProt P45704 · AlphaFold DB P45704
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