› 2j7m

X-ray diffraction
2.3Å resolution

Characterization of a Family 32 CBM

Released:
DOI: 10.2210/pdb2j7m/pdb
PDB entry 2j7m coloured by chain, front view.
PDB entry 2j7m coloured by chain, side view.
PDB entry 2j7m coloured by chain, top view.
Source organism: Clostridium perfringens
Primary publication:
The interaction of a carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor.
Ficko-Blean E, Boraston AB
J Biol Chem 281 37748-57 (2006)
PMID: 16990278

Function and Biology Details

Reaction catalysed: 
[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine
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-171162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
O-GlcNAcase NagJ Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.29 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0TR53 (Residues: 623-767; Coverage: 15%)
Gene names: CPF_1442, nagJ
Sequence domains: F5/8 type C domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

Carbohydrate polymer : NEW Components: NDG, GAL, FUC
Carbohydrate polymer
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 77.315Å b: 77.315Å c: 74.162Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.251
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Carbohydrate-binding domains: multiplicity of biological roles.
Guillén et al. (2010)
6 more

2 mentions without citation

Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens.
Ficko-Blean et al. (2009)
1 more