Research workbench
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase D (Q5ZNB1)
Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase D (Q5ZNB1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5ZNB1
- Type
- protein
- Length
- 407 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC51AAe4Cb53B659c60B10bbf8c60DBDcfBeBfafd
- Molecule
- Endo-1,4-beta-xylanase D
- UniProt
- Q5ZNB1
- Pockets
- 1 · best druggability 0.66
Structure
1 distinct chain · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase D | protein | 407 | 35% helix, 20% strand | Q5ZNB1 |
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 | 313 | 0.66 | 0.81 | 49 | empty |
Modifications
Observed in the structure: 4 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 Q5ZNB1
- Elsewhere: UniProt Q5ZNB1 · AlphaFold DB Q5ZNB1
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