AmpC beta-lactamase N289A mutant in complex with a boronic acid deacylation transition state analog compound SM3

(1R)-1-(2-THIENYLACETYLAMINO)-1-PHENYLMETHYLBORONIC ACID

The deacylation mechanism of AmpC beta-lactamase at ultrahigh resolution

POTASSIUM PHOSPHATE BUFFER, pH 8.7, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Heavy atoms were refined anisotropically. Riding hydrogen atoms on protein C atoms and backbone N atoms were added by Shelx automatically. Hydrogen atoms on -OH groups of SER, THR and TYR were modeled when corresponding positive peaks were observed above 1.5 sigma level in hydrogen-omitted Fo-Fc map. Hydrogen atoms positions remained fixed relative to the heavy atoms during refinement.

Each asymmetric unit contains two protein monomers. The protein functions as a monomer

AmpC; beta-lactamase; deacylation; transition state; boronic acid, HYDROLASE