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X-ray diffraction
0.9Å resolution

ATOMIC RESOLUTION STRUCTURE OF NATIVE ENDOTHIAPEPSIN

Released:

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.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endothiapepsin Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 33.8 KDa
Source organism: Cryphonectria parasitica
UniProt:
  • Canonical: P11838 (Residues: 90-419; Coverage: 83%)
Gene names: EAPA, EPN-1
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P21
Unit cell:
a: 42.72Å b: 74.66Å c: 42.55Å
α: 90° β: 97.27° γ: 90°
R-values:
R R work R free
0.121 not available 0.147