› 1isx

X-ray diffraction
2.1Å resolution

Crystal structure of xylanase from Streptomyces olivaceoviridis E-86 complexed with xylotriose

Released:
DOI: 10.2210/pdb1isx/pdb
PDB entry 1isx coloured by chain, front view.
PDB entry 1isx coloured by chain, side view.
PDB entry 1isx coloured by chain, top view.
Source organism: Streptomyces olivaceoviridis
Primary publication:
Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module.
Fujimoto Z, Kuno A, Kaneko S, Kobayashi H, Kusakabe I, Mizuno H
J Mol Biol 316 65-78 (2002)
PMID: 11829503

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Beta-xylanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 436 amino acids
Theoretical weight: 46.79 KDa
Source organism: Streptomyces olivaceoviridis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7SI98 (Residues: 1-436; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
1 bound ligand:
Ligand XYP 2 x XYP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 75.37Å b: 94.46Å c: 138.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.24
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
Boraston et al. (2004)
4 more

4 mentions without citation

Mapping glycoside hydrolase substrate subsites by isothermal titration calorimetry.
Zolotnitsky et al. (2004)
3 more