Sandbox Reserved 1691
From Proteopedia
(Difference between revisions)
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<scene name='89/892734/Amino_acids_156-159/1'>Amino_acids 156-159</scene> are important part of drug binding site <ref>33172890 </ref>. | <scene name='89/892734/Amino_acids_156-159/1'>Amino_acids 156-159</scene> are important part of drug binding site <ref>33172890 </ref>. | ||
== Structural highlights == | == Structural highlights == | ||
- | + | The protein is 90% transparent. The <scene name='89/892734/Secondary_structure_view_1/1'>secondary structure</scene> contains 77% alpha-helices, 23% beta-sheets. More specific is 13 secondary structural elements of which 10 are alpha helices and 3 are beta-sheets. Alpha helix contains 3 catalytic amino acids, and beta-sheet contains the other one catalytic acid. | |
- | Alpha helix contains | + | |
== Other important features == | == Other important features == | ||
Revision as of 07:48, 7 December 2021
This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699. |
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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
- ↑ 33172890