PDBe 1pj8

X-ray diffraction
2.2Å resolution

Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A 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)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Proteinase K Chain: A
Molecule details ›
Chain: A
Length: 279 amino acids
Theoretical weight: 28.93 KDa
Source organism: Parengyodontium album
UniProt:
  • Canonical: P06873 (Residues: 106-384; Coverage: 76%)
Gene name: PROK
Sequence domains: Subtilase family
Structure domains: Rossmann fold
6-residue peptide (N-Ac-PAPFPA-NH2) Chain: I
Molecule details ›
Chain: I
Length: 7 amino acids
Theoretical weight: 597 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CU K-ALPHA
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
0.17 0.17 not available
Expression system: Not provided