› 1v6u

X-ray diffraction
2.1Å resolution

Crystal Structure Of Xylanase From Streptomyces Olivaceoviridis E-86 Complexed With 2(2)-alpha-L-arabinofuranosyl-xylobiose

Released:
DOI: 10.2210/pdb1v6u/pdb
PDB entry 1v6u coloured by chain, front view.
PDB entry 1v6u coloured by chain, side view.
PDB entry 1v6u coloured by chain, top view.
Source organism: Streptomyces olivaceoviridis
Primary publication:
Crystal structures of decorated xylooligosaccharides bound to a family 10 xylanase from Streptomyces olivaceoviridis E-86.
Fujimoto Z, Kaneko S, Kuno A, Kobayashi H, Kusakabe I, Mizuno H
J Biol Chem 279 9606-14 (2004)
PMID: 14670957

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, AHR
Carbohydrate polymer
2 bound ligands:
Ligand XYP 2 x XYP
Ligand XYS 1 x XYS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 75.29Å b: 94.23Å c: 137.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.253
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structural determinants of the substrate specificities of xylanases from different glycoside hydrolase families.
Pollet et al. (2010)
2 more

2 mentions without citation

Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.
Nordberg Karlsson et al. (2018)
1 more