PDBe 2cbi

X-ray diffraction
2.25Å resolution

Structure of the Clostridium perfringens NagJ family 84 glycoside hydrolase, a homologue of human O-GlcNAcase

Released:

Function and Biology Details

Reactions catalysed:
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. 
(1) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine. (2) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H(2)O = [protein]-L-threonine + N-acetyl-D-glucosamine. 
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
O-GlcNAcase NagJ Chains: A, B
Molecule details ›
Chains: A, B
Length: 594 amino acids
Theoretical weight: 66.69 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0TR53 (Residues: 31-624; Coverage: 61%)
Gene names: CPF_1442, nagJ
Sequence domains:
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: I212121
Unit cell:
a: 119.939Å b: 147.38Å c: 157.687Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.169 0.22
Expression system: Escherichia coli