› 3vsv

X-ray diffraction
1.48Å 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
Macromolecule:
Xylosidase 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

2 bound ligands:
Ligand XYP 26 x XYP
Ligand XYS 9 x XYS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21
Unit cell:
a: 88.779Å b: 201.948Å c: 100.105Å
α: 90° β: 99.18° γ: 90°
R-values:
R R work R free
0.15 0.15 0.168
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

1 mention without citation

The substrate/product-binding modes of a novel GH120 β-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485.
Huang et al. (2012)