Figure 4
(a) Close-up view of the FAD binding site. The residues that participate in the hydrogen bond and van der Waals interactions are shown as stick model and coloured cyan. The bound FAD is coloured yellow. (b) Superposition of the FAD and NAD binding site of apo with the NAD-complex form of OsMDHAR (cyan and grey, respectively). The FAD and NAD of apo structure are coloured yellow and green, respectively, and only FAD of NAD-complex structure is shown as a stick model and coloured grey. The side chains are shown for the positions of the ‘Tyr174’, ‘His315’, and ‘Phe348’ residues, which display the largest conformational changes upon NAD binding. (c) Close-up view of the NAD binding site. The residues participating in the hydrogen bond are shown as a stick model. Note that the predicted 2′-phosphate group of NADP overlaps with Glu196. (d) Close-up view near 2′-phosphate group in NADP bound structure. For clarity, only Ala196 is shown as a stick model. The Glu196 of OsMDHAR-NAD is shown as a stick model and coloured cyan. The 2′-phosphoryl group of NADP is highlighted by circle. All of the hydrogen bonding is within a distance of 3.5 Å.
