Sandbox Reserved 1635
From Proteopedia
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6YSA is found in plants called, Arabidopsis thaliana. 6YSA is important because it's dual protease and ligase activity. These enzymes have become biotechnical interest. Their dual protease and ligase activites are still not well known about today. That this particular protein is heavily researched today. | 6YSA is found in plants called, Arabidopsis thaliana. 6YSA is important because it's dual protease and ligase activity. These enzymes have become biotechnical interest. Their dual protease and ligase activites are still not well known about today. That this particular protein is heavily researched today. | ||
== Important amino acids == | == Important amino acids == | ||
- | Important amino acids within this protein are asparagine, histidine, and cysteine. Most of the amino acids are bound together by hydrogen bonds. Amino acids form the catalytic residues that lower activation energy in an enzyme-catalyzed reaction. | + | Important amino acids within this protein are asparagine, histidine, and cysteine. Most of the amino acids are bound together by hydrogen bonds. Amino acids form the catalytic residues that lower activation energy in an enzyme-catalyzed reaction <scene name='86/861617/Amino_acids/1'>Amino Acids</scene>. |
== Structural highlights == | == Structural highlights == | ||
In the secondary structure, there are 10 alpha helices <scene name='86/861617/Secondary_structure/2'>Secondary Structure</scene>. The tertiary structure contains Citric Acid (CIT) and Sulfate Ion (SO4). There are many Hydrophobic Parts with this protein. <scene name='86/861617/Hydrophobic_parts/1'>Hydrophobic Parts</scene>. Most of the protein is hydrophobic which is all the purple parts. | In the secondary structure, there are 10 alpha helices <scene name='86/861617/Secondary_structure/2'>Secondary Structure</scene>. The tertiary structure contains Citric Acid (CIT) and Sulfate Ion (SO4). There are many Hydrophobic Parts with this protein. <scene name='86/861617/Hydrophobic_parts/1'>Hydrophobic Parts</scene>. Most of the protein is hydrophobic which is all the purple parts. |
Current revision
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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Structure
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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