CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.40 | Beta Barrel | |
2.40.70 | Cathepsin D, subunit A; domain 1 | |
2.40.70.10 | Acid Proteases |
Domain Context
CATH Clusters
Superfamily | Acid Proteases |
Functional Family | Endothiapepsin |
Enzyme Information
3.4.23.22 |
Endothiapepsin.
based on mapping to UniProt P11838
Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.
-!- From the ascomycete Endothia parasitica. -!- Belongs to peptidase family A1. -!- Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.10.
|
UniProtKB Entries (1)
P11838 |
CARP_CRYPA
Cryphonectria parasitica
Endothiapepsin
|
PDB Structure
PDB | 3WZ6 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Tracing binding modes in hit-to-lead optimization: chameleon-like poses of aspartic protease inhibitors
Angew.Chem.Int.Ed.Engl.
|