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Structure paper

TitleOpen-close structural change upon ligand binding and two magnesium ions required for the catalysis of N-acetylhexosamine 1-kinase
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1854, Page 333-340, Year 2015
Publish dateSep 19, 2014 (structure data deposition date)
AuthorsSato, M. / Arakawa, T. / Nam, Y.W. / Nishimoto, M. / Kitaoka, M. / Fushinobu, S.
External linksBiochim. Biophys. Acta / PubMed:25644306
MethodsX-ray diffraction
Resolution1.8 - 2.05 Å
Structure data

PDB-4wh1:
N-Acetylhexosamine 1-kinase (ligand free)
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-4wh2:
N-acetylhexosamine 1-kinase in complex with ADP
Method: X-RAY DIFFRACTION / Resolution: 1.847 Å

PDB-4wh3:
N-acetylhexosamine 1-kinase in complex with ATP
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-ACY:
ACETIC ACID

ChemComp-HOH:
WATER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

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

Source
  • bifidobacterium longum subsp. longum jcm 1217 (bacteria)
KeywordsTRANSFERASE / NahK / anomeric kinase / APH / open conformation

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