Sandbox Reserved 1759

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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 ==
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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 helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. Each subunit contains 9 alpha helix and 15 beta sheets. In the first subunit, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet. The alpha helixes and beta sheets loop and fold to form a 3D globular protein.
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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 helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. Each subunit contains 9 alpha helix and 15 beta sheets. In the first subunit, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>.

Revision as of 00:16, 12 December 2022

Mevalonate 3,5-Bisphosphate Decarboxylase Structure

Caption for this structure

Drag the structure with the mouse to rotate

References

[1]

  1. 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
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