Fig. 2
From: Resistance to aztreonam-avibactam due to a mutation of SHV-12 in Enterobacter
Binding of AVI to SHV-12 and its variant SHV-12R. The residues interact with AVI are depicted in blue. The amino acid substitution is s depicted in purple and the rest of the protein is in green. Molecular docking of SHV-12 and AVI was modeled using AutoDock 4.2.6 [17]. Docking structure was visualized using Pymol (www.pymol.org). Panel A and C, hydrogen bonds of AVI to SHV-12. Ser70 is the active site to hydrolyze β-lactams. Arg244 and several other amino acids, e.g., Ser130, Asn132, and Thr235, formed hydrogen bonds (shown as a cyan region in panel C) to AVI. Panel B and D, hydrogen bonds of AVI to SHV-12R. The Arg244Gly substitution, indicated by an arrow in panel D, altered hydrogen bonds (shown as a cyan region in panel D) of AVI compared to that in SHV-12 (panel A)