Fig. 5: Binding mode of N-palmitoyl FB1.
From: Structural basis of the mechanism and inhibition of a human ceramide synthase
a, Close-up view of the CerS6 active site in the covalent acyl–enzyme intermediate and N-palmitoyl FB1-bound states, showing the transfer of the palmitoyl chain from His211 to the toxin. b, Cytoplasmic portion of the central cavity, viewed from the membrane plane. Residues lining the cavity are shown as sticks. Polar interactions between the carboxylates of the TCA groups of FB1 and positively charged residues on TM2 and TM7 are shown as dashed lines. c, Active site, viewed from the plane of the membrane. d, Polar and nonpolar surfaces on the cytoplasmic half of the central cavity. Cutaway molecular surface view, showing that the hydrocarbon chain of FB1 interacts with the large hydrophobic face formed by TM5–TM7.
