CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.130 | 7 Propeller |
|
2.130.10 | Methylamine Dehydrogenase; Chain H |
|
2.130.10.120 | Prolyl oligopeptidase, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Prolyl oligopeptidase, N-terminal domain |
| Functional Family | Prolyl endopeptidase |
Enzyme Information
| 3.4.21.26 |
Prolyl oligopeptidase.
based on mapping to UniProt P23687
Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.
-!- Found in vertebrates, plants and Flavobacterium. -!- Generally cytosolic, commonly activated by thiol compounds. -!- Belongs to peptidase family S9A. -!- Formerly EC 3.4.22.18.
|
UniProtKB Entries (1)
| P23687 |
PPCE_PIG
Sus scrofa
Prolyl endopeptidase
|
PDB Structure
| PDB | 1UOO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Electrostatic Environment at the Active Site of Prolyl Oligopeptidase is Highly Influential During Substrate Binding
J.Biol.Chem.
|
