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TitleStructural and Mechanistic Characterization of l-Histidinol Phosphate Phosphatase from the Polymerase and Histidinol Phosphatase Family of Proteins.
Journal, issue, pagesBiochemistry, Vol. 52, Page 1101-1112, Year 2013
Publish dateJul 29, 2012 (structure data deposition date)
AuthorsGhodge, S.V. / Fedorov, A.A. / Fedorov, E.V. / Hillerich, B. / Seidel, R. / Almo, S.C. / Raushel, F.M.
External linksBiochemistry / PubMed:23327428
MethodsX-ray diffraction
Resolution1.32 - 1.933 Å
Structure data

PDB-4gc3:
Crystal structure of L-HISTIDINOL PHOSPHATE PHOSPHATASE (HISK) from Lactococcus lactis subsp. lactis Il1403 complexed with ZN and sulfate
Method: X-RAY DIFFRACTION / Resolution: 1.32 Å

PDB-4gk8:
Crystal structure of histidinol phosphate phosphatase (HISK) from Lactococcus lactis subsp. lactis Il1403 complexed with ZN and L-histidinol arsenate
Method: X-RAY DIFFRACTION / Resolution: 1.933 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GK8:
{[(2S)-2-amino-3-(1H-imidazol-5-yl)propyl]oxy}(trihydroxy)-lambda~5~-arsanyl

ChemComp-CL:
Unknown entry

ChemComp-IMD:
IMIDAZOLE

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • lactococcus lactis subsp. lactis (lactic acid bacteria)
KeywordsHYDROLASE / PHP fold / phosphate

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