X-ray diffraction
1.43Å resolution

Endothiapepsin structure obtained at 100K with fragment BTB09871 bound

Source organism: Cryphonectria parasitica
Entry authors: Engilberge S, Huang C-Y, Smith KML, Eris D, Marsh M, Wang M, Wojdyla JA

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: 330 amino acids
Theoretical weight: 33.81 KDa
Source organism: Cryphonectria parasitica
  • Canonical: P11838 (Residues: 90-419; Coverage: 83%)
Gene names: EAPA, EPN-1
Sequence domains: Eukaryotic aspartyl protease

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 45.281Å b: 73.727Å c: 53.042Å
α: 90° β: 109.74° γ: 90°
R R work R free
0.154 0.153 0.181