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. Author manuscript; available in PMC: 2007 Apr 10.
Published in final edited form as: Arch Biochem Biophys. 2007 Jan 9;458(2):194–201. doi: 10.1016/j.abb.2006.12.023

Figure 4.

Figure 4

Stereo figure modeling of inhibitors bound in the active site of MTHFS in the presence of ATP. Inhibitors include: 5-formyl,10-methylTHF (red), 5-formyl,11-methylTHHF (light red), 10-formylTHF (green), 10-formyl THHF (light green), folic acid (yellow). MTHFS is shown in semitransparent spacefilling form, colored gray, except for residues coordinating the pterin ring, which are partially blue, those which potentially make H-bonds to the glutamate moiety, whose side-chains are magenta, and tyrosines 151 and 152, whose side-chains are green. Of the blue residues, it appears that Glu 64 and the main chain O of Asp 59 (on the right side of the figure) can interact with all the inhibitors, while Ser 97 and Gln 58 only coordinate some of them. The figure was rendered using Molscript [20] and Raster3D [21].