2hpj

X-ray diffraction
1.7Å resolution

Crystal structure of the PUB domain of mouse PNGase

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-191601 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.11 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JI78 (Residues: 12-110; Coverage: 15%)
Gene name: Ngly1
Sequence domains: PUB domain
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU, NSLS BEAMLINE X26C
Spacegroup: C2
Unit cell:
a: 66.641Å b: 52.042Å c: 34.946Å
α: 90° β: 115.25° γ: 90°
R-values:
R R work R free
0.149 0.147 0.177
Expression system: Escherichia coli