› 3w6f

X-ray diffraction
2.1Å resolution

Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) in complex with disaccharide

Released:
DOI: 10.2210/pdb3w6f/pdb
PDB entry 3w6f coloured by chain, front view.
PDB entry 3w6f coloured by chain, side view.
PDB entry 3w6f coloured by chain, top view.
Source organism: Ralstonia sp. A-471
Primary publication:
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 T, Kawamoto N, Shinya S, Okazaki N, Nakazawa M, Miyatake K, Fukamizo T, Ueda M, Tamada T
J Biol Chem 288 18696-706 (2013)
PMID: 23658014

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-503399 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Chitin-binding type-3 domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 183 amino acids
Theoretical weight: 20.34 KDa
Source organism: Ralstonia sp. A-471
Expression system: Escherichia coli
UniProt:
  • Canonical: B7XCV4 (Residues: 89-252; Coverage: 75%)
Sequence domains: Transglycosylase SLT domain
Structure domains: Lysozyme

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P6122
Unit cell:
a: 99.304Å b: 99.304Å c: 242.406Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.242
Expression system: Escherichia coli

Quick links

Citations

4 review citations

From bacteria to human: a journey into the world of chitinases.
Adrangi et al. (2013)
3 more

1 mention 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)