› 2cjl

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES

Released:
DOI: 10.2210/pdb2cjl/pdb
PDB entry 2cjl coloured by chain, front view.
PDB entry 2cjl coloured by chain, side view.
PDB entry 2cjl coloured by chain, top view.
Source organism: Streptomyces coelicolor
Primary publication:
Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes.
Hoell IA, Dalhus B, Heggset EB, Aspmo SI, Eijsink VG
FEBS J 273 4889-900 (2006)
PMID: 17010167

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183996 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoside hydrolase family 19 catalytic domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 204 amino acids
Theoretical weight: 21.98 KDa
Source organism: Streptomyces coelicolor
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8CK55 (Residues: 41-244; Coverage: 95%)
Gene names: SCF34.01, SCO0482, chiG
Sequence domains: Chitinase class I
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 48.671Å b: 74.378Å c: 64.179Å
α: 90° β: 108.57° γ: 90°
R-values:
R R work R free
0.188 0.187 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications.
Khan et al. (2015)
1 more

6 mentions without citation

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