› 2drq

X-ray diffraction
2.1Å resolution

Crystal structure of reducing-end-xylose releasing exo-oligoxylanase D263G mutant

Released:
DOI: 10.2210/pdb2drq/pdb
PDB entry 2drq coloured by chain, front view.
PDB entry 2drq coloured by chain, side view.
PDB entry 2drq coloured by chain, top view.
Source organism: Alkalihalobacillus halodurans C-125
Primary publication:
Structural explanation for the acquisition of glycosynthase activity.
Hidaka M, Fushinobu S, Honda Y, Wakagi T, Shoun H, Kitaoka M
J Biochem 147 237-44 (2010)
PMID: 19819900

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Reducing end xylose-releasing exo-oligoxylanase Chain: A
Molecule details ›
Chain: A
Length: 396 amino acids
Theoretical weight: 46.07 KDa
Source organism: Alkalihalobacillus halodurans C-125
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KB30 (Residues: 1-388; Coverage: 100%)
Gene name: BH2105
Sequence domains: Glycosyl hydrolases family 8
Structure domains: Glycosyltransferase

Ligands and Environments

2 bound ligands:
Ligand NI 1 x NI
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 52.206Å b: 85.297Å c: 86.957Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.142 0.194
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Enzymatic synthesis using glycoside phosphorylases.
O'Neill et al. (2015)
7 other articles

1 mention without citation

Crystallization and preliminary X-ray analysis of a cold-active endo-β-1,4-D-xylanase from glycoside hydrolase family 8.
Schoepe et al. (2011)