2f4o

X-ray diffraction
2.26Å resolution

The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs

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:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero hexamer
PDBe Complex ID:
PDB-CPX-157083 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 34.87 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JI78 (Residues: 164-450; Coverage: 44%)
Gene name: Ngly1
Sequence domains: Transglutaminase-like superfamily
Structure domains:
UV excision repair protein RAD23 homolog B Chain: B
Molecule details ›
Chain: B
Length: 61 amino acids
Theoretical weight: 7.19 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P54728 (Residues: 273-332; Coverage: 14%)
Gene names: Mhr23b, Rad23b
Sequence domains: XPC-binding domain
Structure domains: XPC-binding domain
PHQ-VAL-ALA-ASP-CF0 Chain: I
Molecule details ›
Chain: I
Length: 5 amino acids
Theoretical weight: 472 Da

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 96.958Å b: 52.097Å c: 80.848Å
α: 90° β: 113.5° γ: 90°
R-values:
R R work R free
0.22 0.22 0.293
Expression system: Escherichia coli