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 |
Enzyme Information
| 3.4.14.2 |
Dipeptidyl-peptidase II.
based on mapping to UniProt Q9UHL4
Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.
-!- A lysosomal serine-type peptidase maximally active at acidic pH. -!- Cleaves Lys-Ala-naphthylamide. -!- Belongs to peptidase family S28.
|
UniProtKB Entries (1)
| Q9UHL4 |
DPP2_HUMAN
Homo sapiens
Dipeptidyl peptidase 2
|
PDB Structure
| PDB | 4EBB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structures of Human DPP7 Reveal the Molecular Basis of Specific Inhibition and the Architectural Diversity of Proline-Specific Peptidases.
Plos One
|
