Fig. 2: Hydrogen bonding patterns of the individual equilibrium states in the active site of CTX-M-14 in the native, BAB and GBE state. | Communications Chemistry

Fig. 2: Hydrogen bonding patterns of the individual equilibrium states in the active site of CTX-M-14 in the native, BAB and GBE state.

From: Time-resolved crystallography of boric acid binding to the active site serine of the β-lactamase CTX-M-14 and subsequent 1,2-diol esterification

Fig. 2: Hydrogen bonding patterns of the individual equilibrium states in the active site of CTX-M-14 in the native, BAB and GBE state.

Stick and cartoon representation (left) as well as 2D-LigPlot+ representation (right) of the active-site amino acid residues highlighting the hydrogen bond network in the native form (a), with bound boric acid (10 s, BAB) to Ser70 (b) and with the bound glycerol boric acid diester (10 s, GBE) (c). Each equilibrium state is displayed individually without overlapping with the initial states. BAB and GBE oxygen atoms are labeled in red. Potential hydrogen bond distances (Å) are indicated by dashed lines.

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