› 2j1a

X-ray diffraction
1.49Å resolution

Structure of CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose

Released:
DOI: 10.2210/pdb2j1a/pdb
PDB entry 2j1a coloured by chain, front view.
PDB entry 2j1a coloured by chain, side view.
PDB entry 2j1a coloured by chain, top view.
Source organism: Clostridium perfringens ATCC 13124
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
Macromolecule:
O-GlcNAcase NagJ Chain: A
Molecule details ›
Chain: A
Length: 150 amino acids
Theoretical weight: 16.41 KDa
Source organism: Clostridium perfringens ATCC 13124
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

2 bound ligands:
Ligand GAL 1 x GAL
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 43.861Å b: 43.861Å c: 139.475Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.201 0.226
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

3 mentions without citation

A novel, noncatalytic carbohydrate-binding module displays specificity for galactose-containing polysaccharides through calcium-mediated oligomerization.
Montanier et al. (2011)
2 more