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. Author manuscript; available in PMC: 2015 Feb 2.
Published in final edited form as: Chem Biol. 2013 Dec 19;21(1):125–135. doi: 10.1016/j.chembiol.2013.11.006

Figure 4. Ternary complex of PhnY with G3P and truncated cofactor NAD+, see also Supplemental Figure S8.

Figure 4

(A) Stereo view of G3P and NAD+ binding to PhnY. All atoms are colored as before. Superimposed is the difference electron density map contoured at 2.5σ in blue, calculated as before. (B) Interactions are shown as green dashes for the binding of (B) G3P with PhnY, and (C) G3P with GAPDH. G3P bonds are colored purple, and enzyme residue bonds are colored brown. The interactions for the G3P phosphoryl oxygen atom and Cβ hydroxyl, which are absent in PhnY, are shown in red dashes. Note the different conformations of G3P in the PhnY active site and GAPDH active site. Figure was generated by LigPlot+ (Laskowski and Swindells, 2011) using refined coordinates of PhnY-G3P-NAD+ complex for panel B, and PDB 2ESD for panel C.