Research workbench
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase C (Q00177)
Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase C (Q00177) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q00177
- Type
- protein
- Length
- 327 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Endo-1,4-beta-xylanase C
- UniProt
- Q00177
- Pockets
- 1 · best druggability 0.30
Structure
1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase C | protein | 327 | 41% helix, 17% strand | Q00177 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.30 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1TA3 · Crystal Structure of xylanase (GH10) in complex with inhibitor (XIP) · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 1TA3 · Crystal structure of xylanase (GH10) in complex with inhibitor (xip) · an experimental structure of the same protein · chain A against B, TM-score 0.92
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 Q00177
- Elsewhere: UniProt Q00177 · AlphaFold DB Q00177
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