CATH Classification

Domain Context

CATH Clusters

Superfamily Acid Proteases
Functional Family Pepsin A

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 1PSN
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of human pepsin and its complex with pepstatin.
Fujinaga, M., Chernaia, M.M., Tarasova, N.I., Mosimann, S.C., James, M.N.
Protein Sci.