› 1bcx

X-ray diffraction
1.81Å resolution

MUTATIONAL AND CRYSTALLOGRAPHIC ANALYSES OF THE ACTIVE SITE RESIDUES OF THE BACILLUS CIRCULANS XYLANASE

Released:
DOI: 10.2210/pdb1bcx/pdb
PDB entry 1bcx coloured by chain, front view.
PDB entry 1bcx coloured by chain, side view.
PDB entry 1bcx coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase.
Wakarchuk WW, Campbell RL, Sung WL, Davoodi J, Yaguchi M
Protein Sci 3 467-75 (1994)
PMID: 8019418

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-140770 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.38 KDa
Source organism: Niallia circulans
Expression system: Not provided
UniProt:
  • Canonical: P09850 (Residues: 29-213; Coverage: 100%)
Gene name: xlnA
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 44.09Å b: 52.71Å c: 78.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 not available
Expression system: Not provided

Quick links

Citations

14 review citations

Structures and mechanisms of glycosyl hydrolases.
Davies et al. (1995)
13 more

14 mentions without citation

Bacterial xylanases: biology to biotechnology.
Chakdar et al. (2016)
13 more