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:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Pepsin A (preferred)
PDBe Complex ID:
PDB-CPX-133553 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pepsin A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 34.47 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Length: 326 amino acids
Theoretical weight: 34.47 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
- Canonical:
P00791 (Residues: 60-385; Coverage: 88%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P6522
Expression system: Not provided
