› 1r87

X-ray diffraction
1.67Å resolution

Crystal structure of the extracellular xylanase from Geobacillus stearothermophilus T-6 (XT6, monoclinic form): The complex of the WT enzyme with xylopentaose at 1.67A resolution

Released:
DOI: 10.2210/pdb1r87/pdb
PDB entry 1r87 coloured by chain, front view.
PDB entry 1r87 coloured by chain, side view.
PDB entry 1r87 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
Macromolecules (3 distinct):
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

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
3 bound ligands:
Ligand ZN 7 x ZN
Ligand CL 2 x CL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: C2
Unit cell:
a: 120.422Å b: 61.221Å c: 89.583Å
α: 90° β: 119.5° γ: 90°
R-values:
R R work R free
0.169 0.169 0.186
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

3 mentions without citation

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