CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.58 | Methane Monooxygenase Hydroxylase; Chain G, domain 1 |
|
1.20.58.80 | Phosphotransferase system, lactose/cellobiose-type IIA subunit |
Domain Context
CATH Clusters
| Superfamily | Phosphotransferase system, lactose/cellobiose-type IIA subunit |
| Functional Family | Ubiquitin carboxyl-terminal hydrolase 8 |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt P40818
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)
| P40818 |
UBP8_HUMAN
Homo sapiens
Ubiquitin carboxyl-terminal hydrolase 8
|
PDB Structure
| PDB | 2A9U |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Amino-terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-specific Protease 8 (USP8).
J.Biol.Chem.
|
