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Sandbox Reserved 800
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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 | + | 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. |
Revision as of 18:38, 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.
