3prk

X-ray diffraction
2.2Å resolution

INHIBITION OF PROTEINASE K BY METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE. AN X-RAY STUDY AT 2.2-ANGSTROMS 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-139287 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proteinase K Chain: E
Molecule details ›
Chain: E
Length: 279 amino acids
Theoretical weight: 28.93 KDa
Source organism: Parengyodontium album
Expression system: Not provided
UniProt:
  • Canonical: P06873 (Residues: 106-384; Coverage: 76%)
Gene name: PROK
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE Chain: I
Molecule details ›
Chain: I
Length: 6 amino acids
Theoretical weight: 477 Da
Source organism: Parengyodontium album
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 68.3Å b: 68.3Å c: 108.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 not available not available
Expression system: Not provided