Research workbench
AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase Z (P10478)
Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase Z (P10478) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P10478
- Type
- protein
- Length
- 837 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Endo-1,4-beta-xylanase Z
- UniProt
- P10478
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase Z | protein | 837 | 31% helix, 23% strand | P10478 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 720 | 0.69 | 0.77 | 63 | empty |
| 2 | 112 | 0.38 | 0.74 | 24 | empty |
| 3 | 52 | 0.24 | 0.72 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1XYZ · A common protein fold and similar active site in two distinct families of beta-glycanases · an experimental structure of the same protein · chain A against A, TM-score 0.38
- 1XYZ · A common protein fold and similar active site in two distinct families of beta-glycanases · an experimental structure of the same protein · chain A against A, TM-score 0.38
- 1JJF · Structural basis for the substrate specificity of the feruloyl esterase domain of the… · an experimental structure of the same protein · chain A against A, TM-score 0.30
- 1JJF · Structural basis for the substrate specificity of the feruloyl esterase domain of the… · an experimental structure of the same protein · chain A against A, TM-score 0.30
- 1JT2 · Structural basis for the substrate specificity of the ferul domain of the cellulosomal… · an experimental structure of the same protein · chain A against A, TM-score 0.30
- 1JT2 · Structural basis for the substrate specificity of the ferul domain of the cellulosomal… · an experimental structure of the same protein · chain A against A, TM-score 0.30
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 P10478
- Elsewhere: UniProt P10478 · AlphaFold DB P10478
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