CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.1050 | Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 |
|
1.20.1050.40 | Endopeptidase. Chain P; domain 1 |
Domain Context
CATH Clusters
| Superfamily | Endopeptidase. Chain P; domain 1 |
| Functional Family | Thimet oligopeptidase 1 |
Enzyme Information
| 3.4.24.15 |
Thimet oligopeptidase.
based on mapping to UniProt P52888
Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues.
-!- Thiol compounds activate at low concentrations. -!- Belongs to peptidase family M3. -!- Formerly EC 3.4.22.19 and EC 3.4.99.31.
|
UniProtKB Entries (1)
| P52888 |
THOP1_HUMAN
Homo sapiens
Thimet oligopeptidase
|
PDB Structure
| PDB | 1S4B |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization
J.Biol.Chem.
|
