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 Q02890
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)
| P32628 |
RAD23_YEAST
Saccharomyces cerevisiae S288C
UV excision repair protein RAD23
|
PDB Structure
| PDB | 3ESW |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase.
Glycobiology
|