PDBe 1bjr

X-ray diffraction
2.44Å resolution

COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN FRAGMENT AND PROTEINASE K

Released:

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):
LACTOFERRIN Chain: I
Molecule details ›
Chain: I
Length: 10 amino acids
Theoretical weight: 814 Da
Source organism: Bubalus bubalis
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: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 44.6Å b: 38.581Å c: 79.22Å
α: 90° β: 105.8° γ: 90°
R-values:
R R work R free
0.167 0.16 0.225