CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.30 | 2-Layer Sandwich | 
|   | 3.30.40 | Herpes Virus-1 | 
|   | 3.30.40.10 | Zinc/RING finger domain, C3HC4 (zinc finger) | 
Domain Context
CATH Clusters
| Superfamily | Zinc/RING finger domain, C3HC4 (zinc finger) | 
| Functional Family | Ubiquitin carboxyl-terminal hydrolase 8 | 
Enzyme Information
| 3.4.19.12 | Ubiquitinyl hydrolase 1. based on mapping to UniProt P50102 Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). -!- Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. -!- Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. -!- Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). -!- Belongs to peptidase family C12. | 
UniProtKB Entries (2)
| P0CG48 | UBC_HUMAN Homo sapiens Polyubiquitin-C | 
| P50102 | UBP8_YEAST Saccharomyces cerevisiae S288C Ubiquitin carboxyl-terminal hydrolase 8 | 
PDB Structure
| PDB | 3MHS | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Structural insights into the assembly and function of the SAGA deubiquitinating module. Science | 
