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. Author manuscript; available in PMC: 2021 Feb 17.
Published in final edited form as: Int J Biol Macromol. 2017 Jun 16;104(Pt A):584–596. doi: 10.1016/j.ijbiomac.2017.06.065

Fig. 5.

Fig. 5.

The mode of adenosine (A) and NADH (B) binding in the cofactor binding site of iTmSAHase. Only side chains involved in polar or hydrophobic interactions and water molecules (red spheres) are shown. Potential hydrogen bonds are indicated by broken lines. The mF0-DFc difference electron density map is contoured at 3.0σ. (C) Illustration of adenosine binding in the cofactor binding pocket. The ligand and protein are shown in space-filling and surface representation, respectively. (D) Illustration of the non-planar conformation of the six-membered ring of the nicotinamide moiety of NADH in close proximity of two alternative conformations of Cys207. The 2mF0-DFc electron density map is contoured at 1.0σ.