› 3a4w

X-ray diffraction
1.8Å resolution

Crystal structures of catalytic site mutants of active domain 2 of thermostable chitinase from Pyrococcus furiosus complexed with chito-oligosaccharides

Released:
DOI: 10.2210/pdb3a4w/pdb
PDB entry 3a4w coloured by chain, front view.
PDB entry 3a4w coloured by chain, side view.
PDB entry 3a4w coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site.
Tsuji H, Nishimura S, Inui T, Kado Y, Ishikawa K, Nakamura T, Uegaki K
FEBS J 277 2683-95 (2010)
PMID: 20553502

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
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186401 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Chitinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 311 amino acids
Theoretical weight: 34.71 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

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand MG 2 x MG
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P212121
Unit cell:
a: 90.005Å b: 91.985Å c: 107.499Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.154 0.174
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Biodegradation and Prospect of Polysaccharide from Crustaceans.
Qiu et al. (2022)
18 other articles

1 mention without citation

A novel thermostable chitinolytic machinery of Streptomyces sp. F-3 consisting of chitinases with different action modes.
Sun et al. (2019)