PDBe 1pek

X-ray diffraction
2.2Å resolution

STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SUBSTRATE-ANALOGUE HEXA-PEPTIDE INHIBITOR 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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Proteinase K Chain: E
Molecule details ›
Chain: E
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
PEPTIDE PRO-ALA-PRO-PHE Chain: C
Molecule details ›
Chain: C
Length: 4 amino acids
Theoretical weight: 430 Da
Source organism: Parengyodontium album
Expression system: Not provided
D-DAL-ALA-NH2 Chain: D
Molecule details ›
Chain: D
Length: 3 amino acids
Theoretical weight: 158 Da
Source organism: Parengyodontium album
Expression system: Not provided

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 68.28Å b: 68.28Å c: 107.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 not available not available
Expression system: Not provided