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 | 1E5O |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Refinement of Four Endothiapepsin Inhibitor Complexes. Crystallographic Studies of Cytochrome Ch from Methylobacterium Extorquens and Inhibitor Complexes of Aspartic Proteinases.
Crystallographic Studies Studies of Cytochrome Ch from Methylobacterium Extorquens and Inhibitor Complexes of Aspartic Proteinases
|
