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TitleCharacterization of an Acinetobacter baumannii Monofunctional Phosphomethylpyrimidine Kinase That Is Inhibited by Pyridoxal Phosphate.
Journal, issue, pagesBiochemistry, Year 2024
Publish dateMar 4, 2015 (structure data deposition date)
AuthorsDe Vitto, H. / Belfon, K.K.J. / Sharma, N. / Toay, S. / Abendroth, J. / Dranow, D.M. / Lukacs, C.M. / Choi, R. / Udell, H.S. / Willis, S. ...De Vitto, H. / Belfon, K.K.J. / Sharma, N. / Toay, S. / Abendroth, J. / Dranow, D.M. / Lukacs, C.M. / Choi, R. / Udell, H.S. / Willis, S. / Barrera, G. / Beyer, O. / Li, T.D. / Hicks, K.A. / Torelli, A.T. / French, J.B.
External linksBiochemistry / PubMed:38306231
MethodsX-ray diffraction
Resolution1.65 - 1.7 Å
Structure data

PDB-4yl5:
Structure of a putative phosphomethylpyrimidine kinase from Acinetobacter baumannii
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-4ywr:
Structure of a putative phosphomethylpyrimidine kinase from Acinetobacter baumannii in non-covalent complex with pyridoxal phosphate
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

Source
  • acinetobacter baumannii is-123 (bacteria)
  • acinetobacter baumannii (bacteria)
KeywordsTRANSFERASE / putative phosphomethylpyrimidine kinase / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / pyridoxal phoshpate

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