› 3n11

X-ray diffraction
1.35Å resolution

Function and Biology Details

Reaction catalysed: 
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112057 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
chitinase Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 36.27 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: D0VV09 (Residues: 28-360; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 18
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 48.515Å b: 76.051Å c: 76.615Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.215
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The chitinolytic machinery of Serratia marcescens--a model system for enzymatic degradation of recalcitrant polysaccharides.
Vaaje-Kolstad et al. (2013)
1 more

8 mentions without citation

Chitinase: diversity, limitations, and trends in engineering for suitable applications.
Oyeleye et al. (2018)
7 more