› 1cns

X-ray diffraction
1.91Å resolution

CRYSTAL STRUCTURE OF CHITINASE AT 1.91A RESOLUTION

Released:
DOI: 10.2210/pdb1cns/pdb
PDB entry 1cns coloured by chain, front view.
PDB entry 1cns coloured by chain, side view.
PDB entry 1cns coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Refined structure of the chitinase from barley seeds at 2.0 a resolution.
Song HK, Suh SW
Acta Crystallogr D Biol Crystallogr 52 289-98 (1996)
PMID: 15299702

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150134 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
26 kDa endochitinase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 243 amino acids
Theoretical weight: 26.05 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: P23951 (Residues: 24-266; Coverage: 100%)
Sequence domains: Chitinase class I
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 69.38Å b: 44.47Å c: 81.49Å
α: 90° β: 111.99° γ: 90°
R-values:
R R work R free
0.186 0.186 0.244

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Citations

1 review citation

Structural and functional evolution of chitinase-like proteins from plants.
Kesari et al. (2015)
12 other articles

4 mentions without citation

Rapid evolution in plant chitinases: molecular targets of selection in plant-pathogen coevolution.
Bishop et al. (2000)
3 more