2dsk

X-ray diffraction
1.5Å resolution

Crystal structure of catalytic domain of hyperthermophilic chitinase from Pyrococcus furiosus

Released:
Source organism: Pyrococcus furiosus
Primary publication:
Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus.
Acta Crystallogr Sect F Struct Biol Cryst Commun 63 7-11 (2007)
PMID: 17183162

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186402 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chitinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 311 amino acids
Theoretical weight: 34.76 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8U1H5 (Residues: 409-717; Coverage: 43%)
Gene name: PF1233
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU, SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 89.959Å b: 92.78Å c: 107.228Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 0.18
Expression system: Escherichia coli