CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.70 | Cathepsin B; Chain A |
|
3.90.70.80 |
Domain Context
CATH Clusters
| Superfamily | 3.90.70.80 |
| Functional Family | Ubiquitin thioesterase OTU1 |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt P43558
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
|
| P43558 |
OTU1_YEAST
Saccharomyces cerevisiae S288C
Ubiquitin thioesterase OTU1
|
PDB Structure
| PDB | 3C0R |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural basis for ubiquitin recognition by the Otu1 ovarian tumor domain protein
J.Biol.Chem.
|
