Sandbox Reserved 1565: Difference between revisions
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Acetate ions, G5P, and GDP ions are <scene name='82/823089/Ligands/1'>ligands</scene> of IMPDH. NAD serves a function as a ligand as is necessary in the hydrolysis of IMP. The phosphates of the G5P, GDP, and NAD (not pictured) ligands interact through hydrogen bonds and hydrophobic interactions (depending on the amino acid residue; see active binding site below). The monocovalent cations that pass through interact with the phosphates as they activate IMPDH. | Acetate ions, G5P, and GDP ions are <scene name='82/823089/Ligands/1'>ligands</scene> of IMPDH. NAD serves a function as a ligand as is necessary in the hydrolysis of IMP. The phosphates of the G5P, GDP, and NAD (not pictured) ligands interact through hydrogen bonds and hydrophobic interactions (depending on the amino acid residue; see active binding site below). The monocovalent cations that pass through interact with the phosphates as they activate IMPDH. | ||
<scene name='82/823089/Catalytic_triad/1'> | The IMPDH <scene name='82/823089/Catalytic_triad/1'>catalytic triad</scene> includes Arg (325), Asn (306), and Asp (272). This is represented by the solid purple structures in the image. This triad is important as it makes cysteine more reactive as a nucleophilic component. This conserved cysteine, Cys334, (Cys331 in human type II IMPDH) induces binding after becoming more reactive. | ||
<scene name='82/823089/Active_site/1'>Active Binding Site</scene> The active binding site includes the Bateman domains, which are components within the TIM barrel. Binding occurs after the catalytic triad makes cysteine more reactive. The cysteines that become more reactive are shown in green in the image, and are closely related to the active binding site. Asp259 (blue) hydrogen bonds with the ribose hydroxyls of NAD (nicotinamide region), and Ser315 (blue) hydrogen bonds to the ribose phosphate through hydroxyl groups. Gly361 and Gly383 (orange) have hydrophobic interactions with the phosphate of the ligand NAD. Other important interactions include Tyr403 hydrogen bonding to ribose phosphate (NAD), and Glu402 and Glu440 hydrogen bonding with the IMP purine ring. | <scene name='82/823089/Active_site/1'>Active Binding Site</scene> The active binding site includes the Bateman domains, which are components within the TIM barrel. Binding occurs after the catalytic triad makes cysteine more reactive. The cysteines that become more reactive are shown in green in the image, and are closely related to the active binding site. Asp259 (blue) hydrogen bonds with the ribose hydroxyls of NAD (nicotinamide region), and Ser315 (blue) hydrogen bonds to the ribose phosphate through hydroxyl groups. Gly361 and Gly383 (orange) have hydrophobic interactions with the phosphate of the ligand NAD. Other important interactions include Tyr403 hydrogen bonding to ribose phosphate (NAD), and Glu402 and Glu440 hydrogen bonding with the IMP purine ring. | ||
