› 1igo

X-ray diffraction
2.2Å resolution

Family 11 xylanase

Released:
DOI: 10.2210/pdb1igo/pdb
PDB entry 1igo coloured by chain, front view.
PDB entry 1igo coloured by chain, side view.
PDB entry 1igo coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Characterization of a family 11 xylanase from Bacillus subtillis B230 used for paper bleaching.
Oakley AJ, Heinrich T, Thompson CA, Wilce MC
Acta Crystallogr D Biol Crystallogr 59 627-36 (2003)
PMID: 12657781

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-181961 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 205 amino acids
Theoretical weight: 22.58 KDa
Source organism: Bacillus subtilis
UniProt:
  • Canonical: Q7SID8 (Residues: 1-205; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 49.19Å b: 52.54Å c: 65.41Å
α: 90° β: 97.83° γ: 90°
R-values:
R R work R free
0.208 0.208 0.272

Quick links

Citations

1 review citation

Xylanases, xylanase families and extremophilic xylanases.
Collins et al. (2005)
14 other articles

6 mentions without citation

Structural analysis of a glycoside hydrolase family 11 xylanase from Neocallimastix patriciarum: insights into the molecular basis of a thermophilic enzyme.
Cheng et al. (2014)
5 more