CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.70 | Cathepsin B; Chain A |
|
3.90.70.10 | Cysteine proteinases |
Domain Context
CATH Clusters
| Superfamily | Cysteine proteinases |
| Functional Family | ubiquitin carboxyl-terminal hydrolase 15 isoform X1 |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q9Y4E8
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)
| Q9Y4E8 |
UBP15_HUMAN
Homo sapiens
Ubiquitin carboxyl-terminal hydrolase 15
|
PDB Structure
| PDB | 6GHA |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel.
J. Biol. Chem.
|