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. Author manuscript; available in PMC: 2010 Apr 13.
Published in final edited form as: Biochemistry. 2009 Feb 3;48(4):676–687. doi: 10.1021/bi801552y

Figure 5.

Figure 5

(A) Depiction of a portion of the glutamine binding pocket involving the interactions of Arg30, His215 and Ser227. Substrate glutamine is at the bottom, and hydrogen bonds are depicted in red dashed lines. The tautomer of His215 appears well-determined by interactions with the charged Arg30 and Asp66 groups. (B) Depiction of a portion of the glutamine binding pocket showing interactions of Tyr211 and Asp212. Waters labeled as W*, in yellow, are outside the immediate glutamine binding pocket and bridge Asp212 with the 3′-A76 nucleotide of tRNA. Juxtaposition of the substrate glutamine (bottom) with tRNA-A76 is depicted with van der Waals surfaces (bottom). (C) Depiction of a portion of the glutamine binding pocket showing interactions of Gln255, Cys229 and Glu257. Again, substrate glutamine is at the bottom of the drawing and selected hydrogen bonds are depicted as red dashed lines.