3app

X-ray diffraction
1.8Å resolution

STRUCTURE AND REFINEMENT OF PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION

Released:
Source organism: Penicillium janthinellum
Primary publication:
Structure and refinement of penicillopepsin at 1.8 A resolution.
J. Mol. Biol. 163 299-361 (1983)
PMID: 6341600

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: A
Molecule details ›
Chain: A
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 bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 97.37Å b: 46.64Å c: 65.47Å
α: 90° β: 115.4° γ: 90°
R-values:
R R work R free
0.126 not available not available
Expression system: Not provided