Function and Biology Details
Reaction catalysed:
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.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Major pepsin inhibitor 3 and Pepsin A (preferred)
PDBe Complex ID:
PDB-CPX-133554 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pepsin A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 34.59 KDa
Source organism: Sus scrofa
UniProt:
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Length: 326 amino acids
Theoretical weight: 34.59 KDa
Source organism: Sus scrofa
UniProt:
- Canonical:
P00791 (Residues: 60-385; Coverage: 88%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Major pepsin inhibitor 3
Molecule details ›
Chain: B
Length: 149 amino acids
Theoretical weight: 16.41 KDa
Source organism: Ascaris suum
Expression system: Escherichia coli
UniProt:
Structure domains: Pepsin inhibitor-3
Length: 149 amino acids
Theoretical weight: 16.41 KDa
Source organism: Ascaris suum
Expression system: Escherichia coli
UniProt:
- Canonical: P19400 (Residues: 21-169; Coverage: 100%)
Structure domains: Pepsin inhibitor-3
