CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.20 | Single Sheet |
|
2.20.25 | N-terminal domain of TfIIb |
|
2.20.25.10 |
Domain Context
CATH Clusters
| Superfamily | 2.20.25.10 |
| Functional Family | peptide-N(4)-(N-acetyl-beta- glucosaminyl)asparagine amidase |
Enzyme Information
| 3.5.1.52 |
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase.
based on mapping to UniProt Q9JI78
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.
-!- Does not act on (GlcNAc)-Asn, because it requires the presence of more than two amino-acid residues in the substrate (cf. EC 3.5.1.26). -!- Formerly EC 3.2.2.18.
|
UniProtKB Entries (1)
| P54728 |
RD23B_MOUSE
Mus musculus
UV excision repair protein RAD23 homolog B
|
PDB Structure
| PDB | 2F4O |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways.
J.Biol.Chem.
|
