PDBe 5pep

X-ray diffraction
2.34Å resolution

X-RAY ANALYSES OF ASPARTIC PROTEASES. II. THREE-DIMENSIONAL STRUCTURE OF THE HEXAGONAL CRYSTAL FORM OF PORCINE PEPSIN AT 2.3 ANGSTROMS RESOLUTION

Released:

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
Macromolecule:
Pepsin A Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 34.47 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00791 (Residues: 60-385; Coverage: 88%)
Gene name: PGA
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: P6522
Unit cell:
a: 67.4Å b: 67.4Å c: 290.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 not available not available
Expression system: Not provided