PDBe 2hd4

X-ray diffraction
2.15Å resolution

Crystal structure of proteinase K inhibited by a lactoferrin octapeptide Gly-Asp-Glu-Gln-Gly-Glu-Asn-Lys at 2.15 A resolution

Released:
Entry authors: Prem Kumar R, Singh AK, Singh N, 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)
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
Lactotransferrin Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 877 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02788 (Residues: 528-535; Coverage: 1%)
Gene names: GIG12, LF, LTF

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: 68.366Å b: 68.366Å c: 108.079Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.171 0.202
Expression system: Not provided