Sandbox Reserved 1756

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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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An ornithine aminotransferase is composed of 50% of alpha helices, 45% of beta sheets, and 5% of other structures.
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 04:30, 21 November 2022

This Sandbox is Reserved from November 4, 2022 through January 1, 2023 for use in the course CHEM 351 Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1755 through Sandbox Reserved 1764.
To get started:
  • Click the edit this page tab at the top. Click on Show preview and then Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Ornithine Aminotransferase

OAT Protein

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ Butrin A, Butrin A, Wawrzak Z, Moran G, Liu D. Determination of the pH-Dependence, Substrate Specificity and Turnovers of Alternative Substrates for Human Ornithine Aminotransferase. J Biol Chem. 2022 Apr 20:101969. doi: 10.1016/j.jbc.2022.101969. PMID:35460691 doi:http://dx.doi.org/10.1016/j.jbc.2022.101969
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