Sandbox Reserved 806
From Proteopedia
(Difference between revisions)
| Line 12: | Line 12: | ||
==Residues== | ==Residues== | ||
| - | Pictured in yellow are the <scene name='56/563218/Hydrophobic_residues_rotated/1'>hydrophobic residues</scene> | + | Pictured in yellow are the <scene name='56/563218/Hydrophobic_residues_rotated/1'>hydrophobic residues</scene>. |
| - | The <scene name='56/563218/Polarcharged_residues/1'>polar, charged residues</scene> are pictured in green | + | The <scene name='56/563218/Polarcharged_residues/1'>polar, charged residues</scene> are pictured in green. |
==Solvent Accessibility== | ==Solvent Accessibility== | ||
<scene name='56/563218/Waters/1'>Water molecules</scene> are pictured in dark blue. They are mostly located between the beta sheets and alpha helices, in a diagonal line, closer to where the monomers connect to form a dimer. | <scene name='56/563218/Waters/1'>Water molecules</scene> are pictured in dark blue. They are mostly located between the beta sheets and alpha helices, in a diagonal line, closer to where the monomers connect to form a dimer. | ||
Revision as of 20:08, 13 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. |
To get started:
More help: Help:Editing |
|
Contents |
Introduction
This is Triosephosphate isomerase, an enzyme in the glycolytic pathway. It is a dimer, but can function as a .
3D Structure
The contains alpha helices (gold) and beta sheets (purple). Overall, it forms a beta barrel motif.
Residues
Pictured in yellow are the . The are pictured in green.
Solvent Accessibility
are pictured in dark blue. They are mostly located between the beta sheets and alpha helices, in a diagonal line, closer to where the monomers connect to form a dimer.
