1ppk

X-ray diffraction
1.8Å resolution

CRYSTALLOGRAPHIC ANALYSIS OF TRANSITION STATE MIMICS BOUND TO PENICILLOPEPSIN: PHOSPHOROUS-CONTAINING PEPTIDE ANALOGUES

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 97.48Å b: 46.55Å c: 66.42Å
α: 90° β: 116.14° γ: 90°
R-values:
R R work R free
0.132 not available not available
Expression system: Not provided