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. Author manuscript; available in PMC: 2007 Dec 3.
Published in final edited form as: Structure. 2007 Jul;15(7):793–805. doi: 10.1016/j.str.2007.05.009

Figure 4.

Figure 4

ATP binding site. Comparison between human TrpRS (A) and B. stearothermophilus TrpRS (B) of the binding site for the ATP phosphates. Among other substitutions, Arg162 in human TrpRS takes the role of Lys195 of the KMSK195S in B. stearothermophilus TrpRS.