Research workbench
AlphaFold monomer V2.0 prediction for exo-1,4-beta-xylosidase xlnd (Q2UR38)
Analyse AlphaFold monomer V2.0 prediction for exo-1,4-beta-xylosidase xlnd (Q2UR38) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2UR38
- Type
- protein
- Length
- 798 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7782F4817b37743d738e9aF842bf74bd50f2015E
- Molecule
- Exo-1,4-beta-xylosidase xlnd
- UniProt
- Q2UR38
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 29% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exo-1,4-beta-xylosidase xlnd | protein | 798 | 29% helix, 19% strand | Q2UR38 |
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 | 68 | 0.74 | 0.98 | 22 | empty |
| 2 | 320 | 0.63 | 0.80 | 26 | empty |
| 3 | 70 | 0.42 | 0.80 | 19 | empty |
| 4 | 132 | 0.41 | 0.75 | 23 | 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 Q2UR38
- Elsewhere: UniProt Q2UR38 · AlphaFold DB Q2UR38
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