› 1h13

X-ray diffraction
1.3Å resolution

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans
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-185994 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cellulase Chain: A
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 46.02 KDa
Source organism: Pseudoalteromonas haloplanktis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8RJN8 (Residues: 22-426; Coverage: 100%)
Gene name: xyl
Sequence domains: Glycosyl hydrolases family 8
Structure domains: Glycosyltransferase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P212121
Unit cell:
a: 50.874Å b: 90.509Å c: 97.228Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.12 0.119 0.146
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Xylanases, xylanase families and extremophilic xylanases.
Collins et al. (2005)
17 more

4 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
3 more