Sandbox Reserved 1565: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 28: | Line 28: | ||
<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. | ||
<scene name='82/823089/Charge_view/2'>IMPDH charge</scene> is not strong, as shown by this view. There are positive and negative components within the structure, but a relatively neutral substance is better received in this mechanism due to a physiological environment. Negatively-charged glutamate and positively-charged histidine within this enzyme play a role within the covalent bindings in the mechanism. | <scene name='82/823089/Charge_view/2'>IMPDH charge</scene> is not strong, as shown by this view. There are positive and negative components within the structure, but a relatively neutral substance is better received in this mechanism due to a physiological environment. Negatively-charged glutamate and positively-charged histidine within this enzyme play a role within the covalent bindings in the mechanism. Covalent binding is necessary to form the covalent intermediate after NAD is reduced (after interacting with the active site residues). | ||
<scene name='82/823089/Composition_view/1'>IMPDH composition</scene> The brown represents a protein, red represents a RNA, and green represents ligands. | <scene name='82/823089/Composition_view/1'>IMPDH composition</scene> The brown represents a protein, red represents a RNA, and green represents ligands. | ||
