Sandbox Reserved 1565: Difference between revisions

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The <scene name='82/823089/Hydrophobicity_view/1'>hydrophobicity</scene> is within the interior of the molecule as the hydrophilic residues are able to interact in a physiological environment. The hydrophobic region of Gly361 and Gly383 interact with the main chain phosphate, further allowing monovalent cation movement. Hydrophilic regions contain amino acid residues that hydrogen-bond, some conserving tertiary structure and others relating to necessary interactions in the active site (see below).

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 molecules 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.

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 (Cysteine shown in image with "active binding site" link).

Sandbox Reserved 1565: Difference between revisions

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 The <scene name='82/823089/Hydrophobicity_view/1'>hydrophobicity</scene> is within the interior of the molecule as the hydrophilic residues are able to interact in a physiological environment. The hydrophobic region of Gly361 and Gly383 interact with the main chain phosphate, further allowing monovalent cation movement. Hydrophilic regions contain amino acid residues that hydrogen-bond, some conserving tertiary structure and others relating to necessary interactions in the active site (see below).
-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 molecules 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.
 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 (Cysteine shown in image with "active binding site" link).