Methionine synthase: Difference between revisions
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==Your Heading Here (maybe something like 'Structure')== | ==Your Heading Here (maybe something like 'Structure')== | ||
This page is being worked on during the Spring 2022 semester. | |||
<StructureSection load='1k7y' size='310' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1k7y' size='310' side='right' caption='Caption for this structure' scene=''> | ||
Revision as of 21:18, 28 March 2022
Your Heading Here (maybe something like 'Structure')Your Heading Here (maybe something like 'Structure')
This page is being worked on during the Spring 2022 semester.
This is a default text for your page Kia Yang/MS. 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 [1] or to the article describing Jmol [2] to the rescue. EC: 2.1.1.13 PDB ID: 1K7Y
FunctionMethionine synthase methylates homocysteine to methionine. Reactions CatalyzedRelevanceStructural highlightsThis 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.
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ReferencesReferences
- ↑ 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
- ↑ Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML. Domain alternation switches B(12)-dependent methionine synthase to the activation conformation. Nat Struct Biol. 2002 Jan;9(1):53-6. PMID:11731805 doi:10.1038/nsb738