PDBe 1qrp

X-ray diffraction
1.96Å resolution

Human pepsin 3A in complex with a phosphonate inhibitor IVA-VAL-VAL-LEU(P)-(O)PHE-ALA-ALA-OME


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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Pepsin A-4 Chain: E
Molecule details ›
Chain: E
Length: 326 amino acids
Theoretical weight: 34.63 KDa
Source organism: Homo sapiens
  • Canonical: P0DJD7 (Residues: 63-388; Coverage: 87%)
Gene name: PGA4
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 71.9Å b: 151.27Å c: 40.79Å
α: 90° β: 90° γ: 90°
R R work R free
0.2 not available not available