Sandbox Reserved 1673
From Proteopedia
(Difference between revisions)
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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. | ||
- | == Function == | + | == Function of your protein == |
AlyC3 is an <scene name='87/873235/Protein_view_2/1'>enzyme</scene> that is plays a role in β-elimination at the glycosidic 1,4-O-linkage in alginate. | AlyC3 is an <scene name='87/873235/Protein_view_2/1'>enzyme</scene> that is plays a role in β-elimination at the glycosidic 1,4-O-linkage in alginate. | ||
- | == Disease == | ||
- | == | + | == Biological relevance and broader implications == |
- | == Structural highlights == | + | == Important amino acids== |
- | + | ||
+ | == Structural highlights == | ||
+ | strands with one disulfide bridge. The most <scene name='87/873235/Important_residues_view/1'>important residues</scene> for binding substrate as well as those involved in catalysis all lie on beta strands in both domains. | ||
+ | |||
+ | == Other important features == | ||
Revision as of 13:56, 7 April 2021
This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682. |
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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
- ↑ Xu F, Chen XL, Sun XH, Dong F, Li CY, Li PY, Ding H, Chen Y, Zhang YZ, Wang P. Structural and molecular basis for the substrate positioning mechanism of a new PL7 subfamily alginate lyase from the Arctic. J Biol Chem. 2020 Sep 23. pii: RA120.015106. doi: 10.1074/jbc.RA120.015106. PMID:32967968 doi:http://dx.doi.org/10.1074/jbc.RA120.015106