X-ray diffraction
2Å resolution

The crystal structure of human pepsin and its complex with pepstatin


Function and Biology Details

Reaction catalysed:
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pepsin A-4 Chain: E
Molecule details ›
Chain: E
Length: 326 amino acids
Theoretical weight: 34.63 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P0DJD7 (Residues: 63-388; Coverage: 87%)
Gene name: PGA4
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Molecule details ›
Chain: I
Length: 6 amino acids
Theoretical weight: 686 Da
Source organism: Streptomyces argenteolus subsp. toyonakensis
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 72.068Å b: 150.972Å c: 40.854Å
α: 90° β: 90° γ: 90°
R R work R free
0.185 0.185 not available
Expression system: Not provided