Sandbox Reserved 1759
From Proteopedia
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==Mevalonate 3,5-Bisphosphate Decarboxylase Structure== | ==Mevalonate 3,5-Bisphosphate Decarboxylase Structure== | ||
<StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='7T71' size='340' side='right' caption='Caption for this structure' scene=''> | ||
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The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet. | The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet. | ||
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</StructureSection> | </StructureSection> | ||
Revision as of 22:37, 9 December 2022
Mevalonate 3,5-Bisphosphate Decarboxylase Structure
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References
- ↑ Azami Y, Hattori A, Nishimura H, Kawaide H, Yoshimura T, Hemmi H. (R)-mevalonate 3-phosphate is an intermediate of the mevalonate pathway in Thermoplasma acidophilum. J Biol Chem. 2014 Jun 6;289(23):15957-67. doi: 10.1074/jbc.M114.562686. Epub 2014, Apr 22. PMID:24755225 doi:http://dx.doi.org/10.1074/jbc.M114.562686
