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. Author manuscript; available in PMC: 2018 Sep 19.
Published in final edited form as: Biochemistry. 2017 Sep 6;56(37):4951–4961. doi: 10.1021/acs.biochem.7b00499

Figure 2.

Figure 2

Structure of the adduct formed after the inactivation of OAT by FCP. Protein atoms are shown as sticks, with oxygen colored red, nitrogen colored blue, and phosphorus colored orange. (A) Active site of OAT with the ternary adduct formed by K292, FCP, and PLP, which is colored yellow (PDB: 5VWO). The dashed lines represent hydrogen bonds or electrostatic interactions between the active site residues of OAT (green) and the adduct. (B) Simulated annealing omit map (Fo – Fc) of the adduct. The omit map is shown as a gray mesh at 3σ. The omit map was generated after FCP, PLP, and K292 had been omitted from the coordinates. (C) Chemical structure of the adduct formed by FCP, PLP, and K292.