2cbj

X-ray diffraction
2.35Å resolution

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

Released:

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

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 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 BL21(DE3)
UniProt:
  • Canonical: Q0TR53 (Residues: 31-624; Coverage: 61%)
Gene names: CPF_1442, nagJ
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: I212121
Unit cell:
a: 129.613Å b: 145.745Å c: 152.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.248
Expression system: Escherichia coli BL21(DE3)