Sandbox Reserved 781
From Proteopedia
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The <scene name='56/563193/Hydrophobic_residues/1'>hydrophobic residues</scene> can be seen here labeled in gray. And the <scene name='56/563193/Hydrophilic_residues/1'>hydrophilic residues</scene> can be seen here in purple. | The <scene name='56/563193/Hydrophobic_residues/1'>hydrophobic residues</scene> can be seen here labeled in gray. And the <scene name='56/563193/Hydrophilic_residues/1'>hydrophilic residues</scene> can be seen here in purple. | ||
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| + | Water molecules are usually tightly bound to enzymes, <scene name='56/563193/Water_accessibility/1'>here</scene> you can see where the water molecules (blue) access phosphoglycerate kinase. You can also see the ligand shown in green. | ||
Revision as of 19:37, 8 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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Introduction
Structure
The overall structure of phosphoglycerate kinase looks like The of this enzyme are shown here. Alpha helices are shown in cyan and beta sheets are shown in orange.
Hydrogen bonds between the backbone of this enzyme are shown in purple. The angle of the h-bonds in the beta sheets indicate whether they are parallel or anti-parallel sheets. Here you can see that there are both parallel and anti-parallel sheets.
The can be seen here labeled in gray. And the can be seen here in purple.
Water molecules are usually tightly bound to enzymes, you can see where the water molecules (blue) access phosphoglycerate kinase. You can also see the ligand shown in green.
