2id8

X-ray diffraction
1.27Å resolution

Crystal structure of Proteinase K

Released:
Source organism: Parengyodontium album
Primary publication:
What can be done with a good crystal and an accurate beamline?
Acta Crystallogr D Biol Crystallogr 62 1475-83 (2006)
PMID: 17139083

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139275 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P43212
Unit cell:
a: 67.55Å b: 67.55Å c: 106.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.124 not available 0.159