PDBe 3er5

X-ray diffraction
1.8Å resolution

THE ACTIVE SITE OF ASPARTIC PROTEINASES

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):
Angiotensin-4 Chain: I
Molecule details ›
Chain: I
Length: 10 amino acids
Theoretical weight: 1.27 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P01017 (Residues: 6-9; Coverage: 40%)
Gene names: AGT, SERPINA8
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

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 43.1Å b: 75.4Å c: 42.8Å
α: 90° β: 97° γ: 90°
R-values:
R R work R free
0.15 0.15 not available
Expression system: Not provided