Mandelate racemase/muconate lactonizing enzyme

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== Structural highlights ==
== Structural highlights ==
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The D-mannonate dehydratase has two domains: the N-terminal α+β domain and a (β/α)<sub>7</sub> β-barrel domain. The active site of the enzyme is found on the interface of the dimer<ref>PMID:179444491</ref>.
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The D-mannonate dehydratase has <scene name='77/775266/Cv/2'>two domains</scene>: the N-terminal α+β domain and a C-terminal (β/α)<sub>7</sub> β-barrel domain. The <scene name='77/775266/Cv/4'>TextToBeDisplayed</scene>active site of the enzyme is found between these two domains<ref>PMID:179444491</ref>. <scene name='77/775266/Cv/5'>Mg coordination site</scene>.
</StructureSection>
</StructureSection>

Revision as of 12:49, 6 December 2017

MRMLP complex with D-mannonate and Mg+2 ion (green) (PDB code 2qjm)

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3D Structures of Mandelate racemase/muconate lactonizing enzyme

Updated on 06-December-2017

References

  1. . PMID:179444491

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Michal Harel, Alexander Berchansky

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