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 | 2VS2 |
| External Links | |
| Method | NEUTRON DIFFRACTION |
| Organism | |
| Primary Citation |
The Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-Ray Diffraction
J.Am.Chem.Soc.
|
