2cm0

X-ray diffraction
1.9Å resolution

The PUB domain functions as a p97 binding module in human peptide N-glycanase.

Released:
Source organism: Homo sapiens

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188548 (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: 10.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96IV0 (Residues: 11-109; Coverage: 15%)
Gene names: NGLY1, PNG1
Sequence domains: PUB domain
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P65
Unit cell:
a: 73.987Å b: 73.987Å c: 32.994Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 0.223
Expression system: Escherichia coli BL21(DE3)