1apv

X-ray diffraction
1.8Å resolution

CRYSTALLOGRAPHIC ANALYSIS OF TRANSITION STATE MIMICS BOUND TO PENICILLOPEPSIN: DIFLUOROSTATINE-AND DIFLUOROSTATONE-CONTAINING PEPTIDES

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Penicillopepsin-1 Chain: E
Molecule details ›
Chain: E
Length: 323 amino acids
Theoretical weight: 33.47 KDa
Source organism: Penicillium janthinellum
Expression system: Not provided
UniProt:
  • Canonical: P00798 (Residues: 1-323; Coverage: 100%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
INHIBITOR ISOVALERYL (IVA)-VAL-VAL-HYDRATED DIFLUOROSTATONE-N-METHYLAMINE Chain: I
Molecule details ›
Chain: I
Length: 5 amino acids
Theoretical weight: 523 Da
Source organism: Penicillium janthinellum
Expression system: Not provided

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 97.52Å b: 46.57Å c: 66.23Å
α: 90° β: 116.03° γ: 90°
R-values:
R R work R free
0.131 not available not available
Expression system: Not provided