Research workbench
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase C (P35811)
Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase C (P35811) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P35811
- Type
- protein
- Length
- 608 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x21f7C119eB7500129A497A533ee353fC35d9745f
- Molecule
- Endo-1,4-beta-xylanase C
- UniProt
- P35811
- Pockets
- 3 · best druggability 0.59
Structure
1 distinct chain · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase C | protein | 608 | 9% helix, 47% strand | P35811 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 545 | 0.59 | 0.73 | 46 | empty |
| 2 | 247 | 0.58 | 0.78 | 26 | empty |
| 3 | 99 | 0.50 | 0.82 | 21 | 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 P35811
- Elsewhere: UniProt P35811 · AlphaFold DB P35811
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