CATH Classification

Domain Context

CATH Clusters

Superfamily Acid Proteases
Functional Family

Enzyme Information

3.4.23.1
Pepsin A.
based on mapping to UniProt P0DJD7
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
-!- The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis. -!- Belongs to peptidase family A1. -!- Formerly EC 3.4.4.1.

UniProtKB Entries (1)

P0DJD7
PEPA4_HUMAN
Homo sapiens
Pepsin A-4

PDB Structure

PDB 3UTL
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases.
Bailey, D., Carpenter, E.P., Coker, A., Coker, S., Read, J., Jones, A.T., Erskine, P., Aguilar, C.F., Badasso, M., Toldo, L., Rippmann, F., Sanz-Aparicio, J., Albert, A., Blundell, T.L., Roberts, N.B., Wood, S.P., Cooper, J.B.
Acta Crystallogr.,Sect.D