Skip to main content
. Author manuscript; available in PMC: 2019 Nov 19.
Published in final edited form as: J Med Chem. 2018 Dec 19;62(2):987–992. doi: 10.1021/acs.jmedchem.8b01723

Figure 3. Hydrophobic surface of AC with a modeled ceramide substrate.

Figure 3.

(A) The surface representation of the hydrophobic areas of the AC in ribbon diagram are colored yellow and the remaining residues are colored in magenta (α-subunit) and in cyan (β-subunit). The locations of the residues mutated in our previous work (black) and that of the residues forming plausible hydrophobic contacts with the substrate d17 moiety (red) are labeled30. (B) Close-up view of the modeled C8 ceramide substrate (d17:1/8:0, ball and stick in orange) interacting with enzyme residues in the substrate-binding area. The positions of several AC catalytic residues, which can form hypothetical interactions with the substrate in the tetrahedral complex, are indicated.