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. Author manuscript; available in PMC: 2019 Feb 28.
Published in final edited form as: FEBS J. 2018 Nov 23;286(1):169–183. doi: 10.1111/febs.14695

Figure 6. Importance of Cys221-bound water to ligand binding by VIM-1.

Figure 6.

A. Mode of ML302F binding to VIM-1 (green) and VIM-2 (pdb 4PVO [30]; blue). Wat3 in VIM-2 structure is in dark red. B. Overlay of ML302F and hydrolysed meropenem complexes with VIM-1. The active site view of the ML302F complex is shown in lighter, and meropenem in darker, shades. C. Overlay of hydrolysed meropenem binding to VIM-1 (darker colours) and NDM-1 (pdb 5N0H [35] [60]; lighter colours). D. Overlay of available VIM crystal structures (details as Figure 1) showing conserved location of Wat3. Colours are as specified. Note how Wat3 mediates interactions of both substrate and inhibitor carboxylate groups with the Cys221 backbone carbonyl, and substitutes for NDM-1 Lys224 in binding the carboxylate of hydrolysed meropenem (Panel C).