FIG 5.

Docking poses of (R)-o-chloromandelonitrile in the binding pockets of the WT enzyme (a) and the MG mutant (c) and of (S)-o-chloromandelonitrile in the binding pockets of the WT (b) and the MG mutant (d). The catalytic triad (C164-E48-K130) is shown with carbon atoms in purple, as well as other critical residues, with carbon atoms in cyan. Distances between (R)-o-chloromandelonitrile or (S)-o-chloromandelonitrile and the catalytic triads are shown by dashed black lines, and H bonds are shown by solid blue lines. (R)- and (S)-o-chloromandelonitrile are shown in stick figures, with carbon atoms in tan and lilac, respectively. The chlorine, sulfur, oxygen, and nitrogen atoms are shown in green, yellow, red and blue, respectively. All of the atoms of G199 are shown, as it does not have a side chain.