2g9f

X-ray diffraction
1.9Å resolution

Crystal structure of intein-tagged mouse PNGase C-terminal domain

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:
Cellular component:

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: 201 amino acids
Theoretical weight: 22.96 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9JI78 (Residues: 451-651; Coverage: 31%)
Gene name: Ngly1
Sequence domains: PNGase C-terminal domain, mannose-binding module PAW
Structure domains: Peptide N glycanase, PAW domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P3221
Unit cell:
a: 40.76Å b: 40.76Å c: 193.663Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.167 0.213
Expression system: Escherichia coli BL21(DE3)