› 1r85

X-ray diffraction
1.45Å resolution

Crystal structure of the extracellular xylanase from Geobacillus stearothermophilus T-6 (XT6): The WT enzyme (monoclinic form) at 1.45A resolution

Released:
DOI: 10.2210/pdb1r85/pdb
PDB entry 1r85 coloured by chain, front view.
PDB entry 1r85 coloured by chain, side view.
PDB entry 1r85 coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Mapping glycoside hydrolase substrate subsites by isothermal titration calorimetry.
Zolotnitsky G, Cogan U, Adir N, Solomon V, Shoham G, Shoham Y
Proc Natl Acad Sci U S A 101 11275-80 (2004)
PMID: 15277671

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154215 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 379 amino acids
Theoretical weight: 43.87 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P40943 (Residues: 29-407; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

4 bound ligands:
Ligand ZN 7 x ZN
Ligand CL 2 x CL
Ligand SO4 3 x SO4
Ligand GOL 19 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2
Unit cell:
a: 121.51Å b: 61.71Å c: 89.09Å
α: 90° β: 119.07° γ: 90°
R-values:
R R work R free
0.126 not available 0.181
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

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

4 mentions without citation

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