PDBe 2dp4

X-ray diffraction
2.9Å resolution

Crystal structure of the complex formed between proteinase K and a human lactoferrin fragment at 2.9 A resolution

Released:
Entry authors: Singh AK, Singh N, Sharma S, Bhushan A, 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: E
Molecule details ›
Chain: E
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
Lactotransferrin Chain: I
Molecule details ›
Chain: I
Length: 8 amino acids
Theoretical weight: 877 Da
Source organism: Homo sapiens
UniProt:
  • Canonical: P02788 (Residues: 528-535; Coverage: 1%)
Gene names: GIG12, LF, LTF

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 68.4Å b: 68.4Å c: 108.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.193 0.235