› 2dbt

X-ray diffraction
3.14Å resolution

Crystal structure of chitinase C from Streptomyces griseus HUT6037

Released:
DOI: 10.2210/pdb2dbt/pdb
PDB entry 2dbt coloured by chain, front view.
PDB entry 2dbt coloured by chain, side view.
PDB entry 2dbt coloured by chain, top view.
Source organism: Streptomyces griseus
Primary publication:
Structural studies of a two-domain chitinase from Streptomyces griseus HUT6037.
Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe T, Nonaka T
J Mol Biol 358 472-84 (2006)
PMID: 16516924

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-129307 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chitin-binding type-3 domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 265 amino acids
Theoretical weight: 28.5 KDa
Source organism: Streptomyces griseus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O50152 (Residues: 30-294; Coverage: 100%)
Gene names: NCTC13033_02762, chiC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EPE 3 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P3221
Unit cell:
a: 153.116Å b: 153.116Å c: 90.031Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.174 0.225
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

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

3 mentions without citation

Crystal structures of the catalytic domain of a novel glycohydrolase family 23 chitinase from Ralstonia sp. A-471 reveals a unique arrangement of the catalytic residues for inverting chitin hydrolysis.
Arimori et al. (2013)
2 more