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Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128. | Ligand OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128. | ||
== Structural highlights == | == Structural highlights == | ||
| - | The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha and 40% beta | + | The Protein is composed of alpha helix, beta sheet, and other structures. The <scene name='93/934003/60_alpha_and_40_beta/1'>protein</scene> consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the structure. 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. |
Revision as of 23:10, 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
