CATH Classification

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 3WZ8
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Tracing binding modes in hit-to-lead optimization: chameleon-like poses of aspartic protease inhibitors
Kuhnert, M., Koster, H., Bartholomaus, R., Park, A.Y., Shahim, A., Heine, A., Steuber, H., Klebe, G., Diederich, W.E.
Angew.Chem.Int.Ed.Engl.