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. Author manuscript; available in PMC: 2018 Sep 7.
Published in final edited form as: J Struct Biol. 2018 Apr 4;203(2):135–141. doi: 10.1016/j.jsb.2018.04.001

Fig. 3.

Fig. 3.

Ternary complex of AmpKR2 G355T/Q364H mutant. (A) Hydrogen bonds between the substrate and the active site of the AmpKR2 G355T/Q364H mutant. The |Fo| – |Fc| omit map of the substrate was superimposed on the final model of the ternary complex of AmpKR2 G355T/Q364H mutant and contoured at 2.5 σ. (B) The 2-methyl-3-oxopentanoyl binding pocket of wild type AmpKR2 (green) and the G355T/Q364H mutant (cyan). (C) Structural comparison of ternary structure of wild type AmpKR2 (green), the ternary structure of the G335T/Q364H mutant (cyan), and the binary structure of the G335T/Q364H mutant (grey).