×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily Acid Proteases
Functional Family

Enzyme Information

3.4.23.1
Pepsin A.
based on mapping to UniProt P00791
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 (2)

P19400
API3_ASCSU
Ascaris suum
Major pepsin inhibitor 3
P00791
PEPA_PIG
Sus scrofa
Pepsin A

PDB Structure

PDB 1F34
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3.
Ng, K.K., Petersen, J.F., Cherney, M.M., Garen, C., Zalatoris, J.J., Rao-Naik, C., Dunn, B.M., Martzen, M.R., Peanasky, R.J., James, M.N.
Nat.Struct.Biol.
CATH-Gene3D is a Global Biodata Core Resource Learn more...