Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU)

Characterization of Substrate Binding and Catalysis in the Potential Antibacterial Target N-Acetylglucosamine-1-Phosphate Uridyltransferase (Glmu).

1.2-1.8M AMMONIUM SULFATE, 2% PEG-400, 0.1M MES PH 5.2 TO 6.5, AND COBALT (II) CHLORIDE 6.25 MM

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

GLMU, CELL WALL, MAGNESIUM, CELL SHAPE, TRANSFERASE, PEPTIDOGLYCAN SYNTHESIS, ASSOCIATIVE MECHANISM, MULTIFUNCTIONAL ENZYME, NUCLEOTIDYLTRANSFERASE, URIDYLATION, METAL-BINDING, ACYLTRANSFERASE