› 3vsu

X-ray diffraction
2.05Å resolution

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106847 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Parallel beta-helix repeat protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 638 amino acids
Theoretical weight: 72.85 KDa
Source organism: Thermoanaerobacterium saccharolyticum JW/SL-YS485
Expression system: Escherichia coli
UniProt:
  • Canonical: A2ICH1 (Residues: 1-638; Coverage: 100%)
Gene name: Tsac_0939
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21
Unit cell:
a: 88.676Å b: 202.313Å c: 100.4Å
α: 90° β: 99.14° γ: 90°
R-values:
R R work R free
0.153 0.153 0.194
Expression system: Escherichia coli

Quick links

Citations

2 review citations

β-xylosidases and α-L-arabinofuranosidases: accessory enzymes for arabinoxylan degradation.
Lagaert et al. (2014)
1 more

5 mentions without citation

β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides.
Rohman et al. (2019)
4 more