Research workbench
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P17137)
Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P17137) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P17137
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x13c90430eE797775A8F5DD42A7B500C58cdAFd0a
- Molecule
- Endo-1,4-beta-xylanase
- UniProt
- P17137
- Pockets
- 1 · best druggability 0.52
Structure
1 distinct chain · 5% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase | protein | 261 | 5% helix, 48% strand | P17137 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.52 | 0.77 | 28 | 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 P17137
- Elsewhere: UniProt P17137 · AlphaFold DB P17137
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