3ptl

X-ray diffraction
1.3Å resolution

Crystal structure of proteinase K inhibited by a lactoferrin nonapeptide, Lys-Gly-Glu-Ala-Asp-Ala-Leu-Ser-Leu-Asp at 1.3 A resolution.

Released:
Entry authors: Shukla PK, Sinha M, Kaur P, 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)
PDBe Complex ID:
PDB-CPX-139288 (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: Peptidase S8/S53 domain
10-mer peptide from Lactoferrin Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.02 KDa
Source organism: Ovis aries
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P43212
Unit cell:
a: 68.054Å b: 68.054Å c: 106.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.25
Expression system: Not provided