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:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Peptide:N-glycanase-Rad23 complex (preferred)
PDBe Complex ID:
PDB-CPX-152412 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
Molecule details ›
Chain: A
Length: 335 amino acids
Theoretical weight: 39.57 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Transglutaminase-like superfamily
Structure domains:
Length: 335 amino acids
Theoretical weight: 39.57 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q02890 (Residues: 8-342; Coverage: 92%)
Sequence domains: Transglutaminase-like superfamily
Structure domains:
UV excision repair protein RAD23
Molecule details ›
Chain: B
Length: 72 amino acids
Theoretical weight: 7.54 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: XPC-binding domain
Structure domains: XPC-binding domain
Length: 72 amino acids
Theoretical weight: 7.54 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P32628 (Residues: 238-309; Coverage: 18%)
Sequence domains: XPC-binding domain
Structure domains: XPC-binding domain
