PDBe 1apt

X-ray diffraction
1.8Å resolution

CRYSTALLOGRAPHIC ANALYSIS OF A PEPSTATIN ANALOGUE BINDING TO THE ASPARTYL PROTEINASE PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION

Released:
Primary publication:
Crystallographic Analysis of a Pepstatin Analogue Binding to the Aspartyl Proteinase Penicillopepsin at 1.8 Angstroms Resolution
Peptides: Structure and Function, Proceedings of the of the Eighth American Peptide Symposium 1 521- (1983)

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.
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-LYSTA-O-ET (LYSTA IS A LYSYL SIDE CHAIN ANALOGUE OF STATIN Chain: I
Molecule details ›
Chain: I
Length: 4 amino acids
Theoretical weight: 501 Da
Source organism: Unidentified
Expression system: Not provided

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 97.57Å b: 46.47Å c: 66.39Å
α: 90° β: 116.15° γ: 90°
R-values:
R R work R free
0.135 not available not available
Expression system: Not provided