› 1qh7

X-ray diffraction
1.78Å resolution

CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE

Released:
DOI: 10.2210/pdb1qh7/pdb
PDB entry 1qh7 coloured by chain, front view.
PDB entry 1qh7 coloured by chain, side view.
PDB entry 1qh7 coloured by chain, top view.
Source organism: Salipaludibacillus agaradhaerens
Primary publication:
Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase.
Sabini E, Sulzenbacher G, Dauter M, Dauter Z, Jørgensen PL, Schülein M, Dupont C, Davies GJ, Wilson KS
Chem Biol 6 483-92 (1999)
PMID: 10381409

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181966 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 207 amino acids
Theoretical weight: 23.16 KDa
Source organism: Salipaludibacillus agaradhaerens
Expression system: Bacillus subtilis
UniProt:
  • Canonical: Q7SIE3 (Residues: 1-207; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand XYP 2 x XYP
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 71.86Å b: 75.36Å c: 78.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.117 0.117 0.176
Expression system: Bacillus subtilis

Quick links

Citations

5 review citations

Glycosidase mechanisms.
Rye et al. (2000)
4 more

4 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
3 more