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 16 |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q9Y5T5
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 (1)
| Q9Y5T5 |
UBP16_HUMAN
Homo sapiens
Ubiquitin carboxyl-terminal hydrolase 16
|
PDB Structure
| PDB | 2I50 |
| External Links | |
| Method | SOLUTION NMR |
| Organism | Escherichia |
| Primary Citation |
Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin.
J.Mol.Biol.
|
