Sandbox Reserved 1640
From Proteopedia
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
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| + | ==Your Heading Here (maybe something like 'Structure and Function')== | ||
| + | <StructureSection load='6ZLK' size='350' side='right' caption='Ligand Binding sites of 6ZLk' scene=''> | ||
== Function of your Protein == | == Function of your Protein == | ||
The specific function of my protein is that it is an enzyme that comes from bacteria called ''Bacillus cereus''. Its main function is to catalyze the chemical reaction by turning UDP-glucose into UDP- galactose in sugar-containing metabolites. It does this by flipping the chiral center. The PBD of this protein in 6ZLK and it contains 3 ligands. The 3 ligands are UGB, NAD, and UGA. I am focussing on is UGB. | The specific function of my protein is that it is an enzyme that comes from bacteria called ''Bacillus cereus''. Its main function is to catalyze the chemical reaction by turning UDP-glucose into UDP- galactose in sugar-containing metabolites. It does this by flipping the chiral center. The PBD of this protein in 6ZLK and it contains 3 ligands. The 3 ligands are UGB, NAD, and UGA. I am focussing on is UGB. | ||
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| + | </StructureSection> | ||
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Revision as of 18:52, 7 December 2020
| This Sandbox is Reserved from 09/18/2020 through 03/20/2021 for use in CHEM 351 Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, IA. This reservation includes Sandbox Reserved 1628 through Sandbox Reserved 1642. |
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Contents |
Your Heading Here (maybe something like 'Structure')
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Biological relevance and broader implications
Important amino acids
Structural highlights
Our protein comes from the Bacillus cereus HuA2-4 organism. It includes the Epimerase domain. Our protein has a fair amount of secondary structures. I see that this protein possesses 12 helices and 12 beta-sheets. This tertiary structure contains many hydrophobic interactions. There are 3 major ligand binding sites.: UGA, NAD, and UGB. This means that the amino acids at the binding sites have nonpolar R groups cluster together, on the inside of the protein. This leaves the hydrophilic amino acids on the outside of the structure. This protein contains a few sugar rings in its metabolic pathway. The process creates sugar products. This enzyme creates a cavity where the sugar group binds and modifies itself. It has one Ramachandran Outlier. the total structure Weight is 153.40 kDa.The way that the protein is folded denotes that it might also be a quaternary structure.
Other important features
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
References
- ↑ 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
- ↑ 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
