PDBe 2er7

X-ray diffraction
1.6Å resolution

X-RAY ANALYSES OF ASPARTIC PROTEINASES.III. THREE-DIMENSIONAL STRUCTURE OF ENDOTHIAPEPSIN COMPLEXED WITH A TRANSITION-STATE ISOSTERE INHIBITOR OF RENIN AT 1.6 ANGSTROMS RESOLUTION

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Endothiapepsin Chain: E
Molecule details ›
Chain: E
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%)
Gene names: EAPA, EPN-1
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
TRANSITION-STATE ISOSTERE INHIBITOR OF RENIN Chain: I
Molecule details ›
Chain: I
Length: 8 amino acids
Theoretical weight: 1.1 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 43Å b: 75.7Å c: 42.9Å
α: 90° β: 97° γ: 90°
R-values:
R R work R free
0.142 0.142 not available
Expression system: Not provided