Sandbox Reserved 800
From Proteopedia
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<Structure load='2akz' size='500' frame='true' align='right' caption='Enolase' scene='Insert optional scene name here' /> | <Structure load='2akz' size='500' frame='true' align='right' caption='Enolase' scene='Insert optional scene name here' /> | ||
This is <scene name='56/563212/Rainbow_enolate/2'>Rainbow Enolate</scene>. Isn't it pretty! :) | This is <scene name='56/563212/Rainbow_enolate/2'>Rainbow Enolate</scene>. Isn't it pretty! :) | ||
| - | This is <scene name='56/563212/Enolate_side_chain_a/1'>Enolate side chain A</scene> with the helixes and sheets represented in different colors.This scene shows the <scene name='56/563212/Hydrophobic_residues/1'>hydrophobic residues</scene> of Enolate. The hydrophobic residues are shown in grey. <scene name='56/563212/Hydrogen_bonding/1'>Hydrogen bonds</scene> are shown in purple while the beta-sheets are shown in yellow. The way that the hydrogen bonds are set up shows that the beta-sheets are parallel in nature, however, there are also anti-parallel beta-sheets at other portions of the molecule. <scene name='56/563212/Solvent_water/1'>Water</scene> is shown in red, with the enzyme in a grey and the ligand is in green. The water is mostly located on the outer edge of the Enolate with some clustering in and around the ligand binding site. The <scene name='56/563212/Interactions_with_ligand/1'>ligand binding site</scene> is shown here. The ligand (Malate) is interacting with mostly polar residues to stabilize malate binding in the pocket with hydrogen bonds. There are also some non-polar side chains that are not involved in hydrogen bonding, but and important in the shape and stability of the binding pocket. | + | This is <scene name='56/563212/Enolate_side_chain_a/1'>Enolate side chain A</scene> with the helixes and sheets represented in different colors.This scene shows the <scene name='56/563212/Hydrophobic_residues/1'>hydrophobic residues</scene> of Enolate. The hydrophobic residues are shown in grey. <scene name='56/563212/Hydrogen_bonding/1'>Hydrogen bonds</scene> are shown in purple while the beta-sheets are shown in yellow. The way that the hydrogen bonds are set up shows that the beta-sheets are parallel in nature, however, there are also anti-parallel beta-sheets at other portions of the molecule. <scene name='56/563212/Solvent_water/1'>Water</scene> is shown in red, with the enzyme in a grey and the ligand is in green. The water is mostly located on the outer edge of the Enolate with some clustering in and around the ligand binding site. The <scene name='56/563212/Interactions_with_ligand/1'>ligand binding site</scene> is shown here. The ligand (Malate) is interacting with mostly polar residues to stabilize malate binding in the pocket with hydrogen bonds. There are also some non-polar side chains that are not involved in hydrogen bonding, but and important in the shape and stability of the binding pocket. The <scene name='56/563212/Catalytic_residues/1'>catalytic residues</scene> |
Revision as of 19:42, 16 October 2013
| This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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PBD: 2AKZ
Catalytic Residus: E 166; H 189; E 209; V 240; K 342; H 370; A 393;
Ligands: G37; A38; S39; T40; I42; H157; Q165; E166; E209; S248; E249; Q297; K342; R371; S372
Metal Ligand Binding Sites: S39; Q165; E166; D244; E242 D317; L340 K342; K393
This Enzyme is a Dimer
Enzyme Reaction 2-phospho-D-glycerate <--> phosphoenolpyruvate + H2O
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This is . Isn't it pretty! :) This is with the helixes and sheets represented in different colors.This scene shows the of Enolate. The hydrophobic residues are shown in grey. are shown in purple while the beta-sheets are shown in yellow. The way that the hydrogen bonds are set up shows that the beta-sheets are parallel in nature, however, there are also anti-parallel beta-sheets at other portions of the molecule. is shown in red, with the enzyme in a grey and the ligand is in green. The water is mostly located on the outer edge of the Enolate with some clustering in and around the ligand binding site. The is shown here. The ligand (Malate) is interacting with mostly polar residues to stabilize malate binding in the pocket with hydrogen bonds. There are also some non-polar side chains that are not involved in hydrogen bonding, but and important in the shape and stability of the binding pocket. The
