Sandbox Reserved 1467
From Proteopedia
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The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices, with some additional beta sheets. | The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices, with some additional beta sheets. | ||
The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, N-domain (navy) and C-Domain (gray). The two domains in this protein, Obc1, mediate oxalogenesis. The N-domain consists of an ObcB activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses. | The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, N-domain (navy) and C-Domain (gray). The two domains in this protein, Obc1, mediate oxalogenesis. The N-domain consists of an ObcB activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses. | ||
- | + | When looking at the <scene name='79/799595/Space_fill/1'>space-filling view of structure </scene> it is hard to distinguish between the different parts of the protein. This view, can give a better insight on the size, shape, and representation of the complete molecule. | |
- | <scene name='79/799595/Space_fill/1'> | + | |
- | + | ||
<scene name='79/799595/Hydrophobic/1'>Hydrophobicity</scene> | <scene name='79/799595/Hydrophobic/1'>Hydrophobicity</scene> | ||
Ligand: | Ligand: |
Revision as of 00:09, 15 November 2018
This Sandbox is Reserved from October 22, 2018 through April 30, 2019 for use in the course Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, IA USA. This reservation includes Sandbox Reserved 1456 through Sandbox Reserved 1470. |
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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