Fig. 3.

Binding of compound 1 in the active site of rat FAAH. (A) Compound 1 in the active site, with electron density shown as a blue mesh and contoured at a level of 1σ from a 2Fo-Fc map. Compound 1 is shown in sticks with atomic color of carbon in yellow, oxygen in red, nitrogen in blue, and bromine in deep purple. The catalytic triad is shown in sticks with carbon in green. The protein is shown in both ribbon and electrostatic molecular surface representations. (B) Compound 1 binding pocket with surrounding residues shown in sticks with carbon atom colored wheat. The corresponding residues, Phe432 and Met436, from the apo FAAH structure are shown in color cyan. (C) Mechanism of the covalent modification of FAAH by compound 1.