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. Author manuscript; available in PMC: 2018 Apr 4.
Published in final edited form as: Biochemistry. 2017 Jun 28;56(27):3454–3462. doi: 10.1021/acs.biochem.7b00194

Figure 4. The binding profiles of SBFI-26 in the canonical sites of FABP5 and FABP7.

Figure 4

(A) The FABP5-SBFI-26 canonical position (cyan). The carboxyl group of SBFI-26 forms a salt bridge with Arg129 and hydrogen bonds with Tyr131 and Arg109. Water molecules are shown as red spheres. (B) In the FABP7-SBFI-26- complex, the carboxyl group of SBFI-26 forms a salt bridge with Arg127 and hydrogen bonds with Tyr129, Arg107, and Thr54. SBFI-26 specific interactions between the carbonyl group and Gly34 and Thr37 are mediated by a water molecule. (C) Hydrophobic interactions between SBFI-26 and FABP7.