Research workbench
AlphaFold monomer V2.0 prediction for putative beta-D-xylosidase (P83344)
Analyse AlphaFold monomer V2.0 prediction for putative beta-D-xylosidase (P83344) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P83344
- Type
- protein
- Length
- 461 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Putative beta-D-xylosidase
- UniProt
- P83344
- Pockets
- 3 · best druggability 0.48
Structure
1 distinct chain · 26% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative beta-D-xylosidase | protein | 461 | 26% helix, 25% strand | P83344 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 166 | 0.48 | 0.77 | 25 | empty |
| 2 | 154 | 0.41 | 0.73 | 24 | empty |
| 3 | 51 | 0.25 | 0.72 | 16 | empty |
Modifications
Observed in the structure: 3 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 P83344
- Elsewhere: UniProt P83344 · AlphaFold DB P83344
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