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).
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).


<scene name='82/823089/Ligands/1'>Ligand View</scene> In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein. Other ligands include G5P and GDP.
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.  


<scene name='82/823089/Catalytic_triad/1'>Catalytic Triad</scene> The IMPDH triad 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/Catalytic_triad/1'>Catalytic Triad</scene> The IMPDH triad 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.
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