Skip to main content
. Author manuscript; available in PMC: 2017 Dec 15.
Published in final edited form as: Arch Biochem Biophys. 2016 Oct 18;612:46–56. doi: 10.1016/j.abb.2016.10.011

Figure 5. β-NADH vs β-NADPH Binding to PpRen.

Figure 5

A. Stereo view of the β-NADH-renalase (PDB: 4ZCC, blue cartoon) overlaid on the NADPH-renalase (structure determined here, green cartoon). FAD is colored with carbon atoms yellow for both molecules. The β-NADH is shown with pink carbon atoms and the NADPH is magenta. The two most proximal residues are shown with carbon atoms green. The phe204 ring stacks with the adenine ring of β-NAD(P)H. The β-carbon of phe204 is 3.9 Å from one oxygen of the 2-phosphoryl group. The amide-nitrogen of gln206 is 3.4 Å from the same oxygen; however, the density is poor for this sidechain. Note that the FAD is buried, and that the β-NAD(P)H is bound to a cleft on the exterior of the protein. B. A simulated annealing omit map contoured at 3σ surrounds the β-NADPH (omitted in calculation) shows that the nicotinamide and nicotinamide-ribose of NADPH are not resolved in the map.