Function and Biology Details
Reaction catalysed:
Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Endothiapepsin and peptide (preferred)
PDBe Complex ID:
PDB-CPX-145959 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Endothiapepsin
Molecule details ›
Chain: E
Length: 330 amino acids
Theoretical weight: 33.81 KDa
Source organism: Cryphonectria parasitica
Expression system: Not provided
UniProt:
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Length: 330 amino acids
Theoretical weight: 33.81 KDa
Source organism: Cryphonectria parasitica
Expression system: Not provided
UniProt:
- Canonical:
P11838 (Residues: 90-419; Coverage: 83%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P21
Expression system: Not provided
