X-ray diffraction
1.15Å resolution

Cocktail experiment E: fragments 52, 58, and 63 at 90 mM concentration in complex with Endothiapepsin

Source organism: Cryphonectria parasitica
Entry authors: Hassaan E, Klebe G, Heine A, Schiebel J, Koester H

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Endothiapepsin Chain: A
Molecule details ›
Chain: A
Length: 419 amino acids
Theoretical weight: 43.28 KDa
Source organism: Cryphonectria parasitica
  • Canonical: P11838 (Residues: 1-419; Coverage: 100%)
Gene names: EAPA, EPN-1
Sequence domains: Eukaryotic aspartyl protease

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 45.401Å b: 73.178Å c: 52.659Å
α: 90° β: 109.762° γ: 90°
R R work R free
0.127 0.127 0.145