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. Author manuscript; available in PMC: 2015 Apr 1.
Published in final edited form as: Bioorg Med Chem. 2014 Mar 3;22(7):2149–2156. doi: 10.1016/j.bmc.2014.02.037

Figure 1.

Figure 1

(A) Tracked distances along the MD trajectory for the CYP2A6-Nic2a binding structure. Nam---Heme(Fe) represents the distance between the nitrogen atom on the amine group of Nic2a and the heme iron atom; Npy---N297(Nδ) represents the distance between the nitrogen atom on the pyridine group of Nic2a and the Nδ atom of the N297 side chain; Nam---G301(O) is the distance between the nitrogen atom on the amine group of Nic2a and the carbonyl oxygen atom on the backbone of residue G310; and Ofu---G301(N) represents the distance between the furan oxygen atom of Nic2a and the backbone nitrogen atom of residue G301. (B) QM/MM-optimized CYP2A6-Nic2a binding structure (optimized at B3LYP/6-31G*:Amber8 level). The structure is represented as ribbon for CYP2A6, stick style for the heme group, and ball-and-stick style for Nic2a. The dashed line represents the averaged distance between the nitrogen atom on the amine group of Nic2a and the heme iron atom based on the 10 QM/MM-optimized structures. (C) Intermolecular interactions in the optimized CYP2A6-Nic2a binding structure. Residues from CYP2A6 within 5 Å of Nic2a are shown in stick style. The hydrogen-bond interaction between the nitrogen atom on the pyridine group of Nic2a and the Hδ atom of N297 side chain is represented as dashed line with labeled averaged distance from the 10 QM/MM-optimized structures, also labeled the averaged distance for the hydrogen bond between the amine group of Nic2a and the backbone carbonyl oxygen of residue G301 based on the 10 QM/MM-optimized structures.