PDBe 4fon

X-ray diffraction
1.05Å resolution

High Energy Remote SAD structure solution of Proteinase K from the 37.8 keV Tellurium K edge

Released:
Source organism: Parengyodontium album
Entry author: Jakoncic J

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)
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: Rossmann fold

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID15C, NSLS BEAMLINE X6A
Spacegroup: P43212
Unit cell:
a: 68.18Å b: 68.18Å c: 102.688Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.113 0.112 0.131