CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.532 | Ubiquitin C-terminal Hydrolase UCH-l3 |
|
3.40.532.10 | Peptidase C12, ubiquitin carboxyl-terminal hydrolase |
Domain Context
CATH Clusters
| Superfamily | Peptidase C12, ubiquitin carboxyl-terminal hydrolase |
| Functional Family | Ubiquitin carboxyl-terminal hydrolase |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt P09936
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)
| P09936 |
UCHL1_HUMAN
Homo sapiens
Ubiquitin carboxyl-terminal hydrolase isozyme L1
|
PDB Structure
| PDB | 2ETL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1.
Proc.Natl.Acad.Sci.USA
|
