1pfg

X-ray diffraction
2.5Å resolution

Strategy to design inhibitors: Structure of a complex of Proteinase K with a designed octapeptide inhibitor N-Ac-Pro-Ala-Pro-Phe-DAla-Ala-Ala-Ala-NH2 at 2.5A resolution

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-139280 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proteinase K Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 28.96 KDa
Source organism: Parengyodontium album
UniProt:
  • Canonical: P06873 (Residues: 106-384; Coverage: 76%)
Gene name: PROK
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
N-Ac-PAPFAAAA-NH2 Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 739 Da
Source organism: Parengyodontium album
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CONVENTIONAL Cu
Spacegroup: P43212
Unit cell:
a: 68Å b: 68Å c: 107.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.167 not available
Expression system: Not provided