PDBe 3osz

X-ray diffraction
2.26Å resolution

Crystal Structure of the complex of proteinase K with an antimicrobial nonapeptide, at 2.26 A resolution

Released:
Entry authors: Singh A, Sinha M, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP

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: 28.96 KDa
Source organism: Parengyodontium album
UniProt:
  • Canonical: P06873 (Residues: 106-384; Coverage: 76%)
Gene name: PROK
Sequence domains: Subtilase family
Structure domains: Rossmann fold
Lactoferrin Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.02 KDa
Source organism: Ovis aries
Expression system: Not provided
UniProt:
  • Canonical: Q5MJE8 (Residues: 405-414; Coverage: 2%)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 68.29Å b: 68.29Å c: 108.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.193
Expression system: Not provided