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:
monomeric (preferred)
Assembly name:
Endothiapepsin (preferred)
PDBe Complex ID:
PDB-CPX-145946 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endothiapepsin
Molecule details ›
Chain: A
Length: 419 amino acids
Theoretical weight: 43.28 KDa
Source organism: Cryphonectria parasitica
UniProt:
Sequence domains: Eukaryotic aspartyl protease
Length: 419 amino acids
Theoretical weight: 43.28 KDa
Source organism: Cryphonectria parasitica
UniProt:
- Canonical:
P11838 (Residues: 1-419; Coverage: 100%)
Sequence domains: Eukaryotic aspartyl protease
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
MAX IV BEAMLINE BioMAX
Spacegroup:
P21
