Sandbox Reserved 1756

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Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein
Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein
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<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>
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Each C=O consists of two oxygen atoms that form hydrogen bonds, which stabilize the secondary structure. A polar amino acid residue is on the outside and a nonpolar amino acid is inside the alpha helix since non-polar amino acids do not react with water. Beta sheet runs in an antiparallel direction of non-polar and polar amino acids.
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<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site
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<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene>
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<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site.
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<scene name='93/934000/Aa_aromatic/1'>Aromatic rings</scene> plays a role important role in protein structure and ligand binding. Aromatic ring is important of protein interaction that allows pi stacking and acts as acceptor for hydrogen bonds. It is important for protein structure and ligand binding.
<scene name='93/934000/Aa_aromatic/1'>Aromatic rings</scene> plays a role important role in protein structure and ligand binding. Aromatic ring is important of protein interaction that allows pi stacking and acts as acceptor for hydrogen bonds. It is important for protein structure and ligand binding.
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<scene name='93/934000/Aa_interactions/1'>Hydrophobic interaction</scene> is important
 
<scene name='93/934000/Aa_polar/1'>
<scene name='93/934000/Aa_polar/1'>

Current revision

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.
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  • 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.
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  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

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Ornithine Aminotransferase

OAT Enzyme

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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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