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Structure paper

TitleKinetic and structural studies of the role of the active site residue Asp235 of human pyridoxal kinase.
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 381, Page 12-15, Year 2009
Publish dateDec 10, 2008 (structure data deposition date)
AuthorsGandhi, A.K. / Ghatge, M.S. / Musayev, F.N. / Sease, A. / Aboagye, S.O. / di Salvo, M.L. / Schirch, V. / Safo, M.K.
External linksBiochem. Biophys. Res. Commun. / PubMed:19351586
MethodsX-ray diffraction
Resolution2.3 - 2.5 Å
Structure data

PDB-3fhx:
Crystal structure of D235A mutant of human pyridoxal kinase
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3fhy:
Crystal structure of D235N mutant of human pyridoxal kinase
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-PXL:
3-HYDROXY-5-(HYDROXYMETHYL)-2-METHYLISONICOTINALDEHYDE

ChemComp-SO4:
SULFATE ION

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / beta sheet with alpha helix / ATP complex / metal ion / ATP-binding / Kinase / Metal-binding / Nucleotide-binding / Acetylation / Alternative splicing / Cytoplasm / Zinc

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