› 2v5d

X-ray diffraction
3.3Å resolution

Structure of a Family 84 Glycoside Hydrolase and a Family 32 Carbohydrate-Binding Module in Tandem from Clostridium perfringens.

Released:
DOI: 10.2210/pdb2v5d/pdb
PDB entry 2v5d coloured by chain, front view.
PDB entry 2v5d coloured by chain, side view.
PDB entry 2v5d coloured by chain, top view.
Source organism: Clostridium perfringens
Primary publication:
Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens.
Ficko-Blean E, Gregg KJ, Adams JJ, Hehemann JH, Czjzek M, Smith SP, Boraston AB
J Biol Chem 284 9876-84 (2009)
PMID: 19193644

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: 737 amino acids
Theoretical weight: 82.33 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q0TR53 (Residues: 31-767; Coverage: 76%)
Gene names: CPF_1442, nagJ
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 46.851Å b: 69.546Å c: 136.78Å
α: 90° β: 95.78° γ: 90°
R-values:
R R work R free
0.325 0.322 0.37
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Insights into the recognition of the human glycome by microbial carbohydrate-binding modules.
Ficko-Blean et al. (2012)
2 more

3 mentions without citation

A proteomic and cellular analysis of uropods in the pathogen Entamoeba histolytica.
Marquay Markiewicz et al. (2011)
2 more