Research workbench
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P48793)
Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P48793) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P48793
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- Endo-1,4-beta-xylanase
- UniProt
- P48793
- Pockets
- 1 · best druggability 0.54
Structure
1 distinct chain · 5% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase | protein | 190 | 5% helix, 62% strand | P48793 |
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 | 239 | 0.54 | 0.77 | 33 | empty |
Compared structures
- 1XND · High-resolution structures of xylanases from B. circulans and T. harzianum identify a new… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 1XND · High-resolution structures of xylanases from B. circulans and T. harzianum identify a new… · an experimental structure of the same protein · chain A against A, TM-score 0.99
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 P48793
- Elsewhere: UniProt P48793 · AlphaFold DB P48793
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