CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.120 | Four Helix Bundle (Hemerythrin (Met), subunit A) |
|
1.20.120.980 | Serine carboxypeptidase S28, SKS domain |
Domain Context
CATH Clusters
| Superfamily | Serine carboxypeptidase S28, SKS domain |
| Functional Family | lysosomal Pro-X carboxypeptidase |
Enzyme Information
| 3.4.16.2 |
Lysosomal Pro-Xaa carboxypeptidase.
based on mapping to UniProt P42785
Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid.
-!- A lysosomal peptidase active at acidic pH that inactivates angiotensin II. -!- Inhibited by diisopropyl fluorophosphate. -!- Belongs to peptidase family S28. -!- Formerly EC 3.4.12.4.
|
UniProtKB Entries (1)
| P42785 |
PCP_HUMAN
Homo sapiens
Lysosomal Pro-X carboxypeptidase
|
PDB Structure
| PDB | 3N2Z |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
Bmc Struct.Biol.
|
