› 1h12

X-ray diffraction
1.2Å 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

2 bound ligands:
Ligand XYP 1 x XYP
Ligand XYS 1 x XYS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 50.972Å b: 90.734Å c: 97.581Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.108 0.107 0.13
Expression system: Escherichia coli

Quick links

Citations

17 review citations

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

20 mentions without citation

Psychrophilic enzymes: from folding to function and biotechnology.
Feller G. (2013)
19 more