Fig. 2
From: Structure and inhibition mechanism of the catalytic domain of human squalene epoxidase
Human SQLE structure and inhibition. a Overall structure of SQLE bound to inhibitor NB-598. SQLE protein is shown in ribbon representation with the FAD-binding domain in green, the substrate-binding domain in magenta, and the C-terminal membrane–associated helical domain in orange. FAD (yellow) and NB-598 (cyan) are shown as sticks. Hetero-atoms follow the color scheme of yellow, blue, red, and orange for sulfur, nitrogen, oxygen, and phosphor, respectively. b NB-598 binding site. NB-598 and FAD are in ball-and-stick presentation with atomic color scheme as described above. The residues forming the compound binding site is in line presentation with the color scheme on carbon atoms to match the domain coloring scheme as in panel a with important specific residues shown as sticks. The van der waals (VDW) contact surface of the pocket within the 4.5 Å of NB-598 shown as semi-translucent surface. Hydrogen bond interaction between Y195 and the central amine of NB-598 is shown as black dashed line with the distance labeled
