Mandelate racemase/muconate lactonizing enzyme

(Difference between revisions)

Revision as of 10:17, 9 July 2019

Updated on 09-July-2019

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 == Structural highlights ==
-The D-mannonate dehydratase has <scene name='77/775266/Cv/6'>two domains</scene>: the <scene name='77/775266/Cv/7'>N-terminal α+β domain</scene> and a <scene name='77/775266/Cv/8'>(β/α)<sub>7</sub> β-barrel domain</scene>. The <scene name='77/775266/Cv/4'>active site</scene> of the enzyme is found between these two domains<ref>PMID:179444491</ref>. <scene name='77/775266/Cv/5'>Mg coordination site</scene>.
+The D-mannonate dehydratase has <scene name='77/775266/Cv/9'>two domains</scene>: the <scene name='77/775266/Cv/10'>N-terminal α+β domain</scene> and a <scene name='77/775266/Cv/11'>(β/α)<sub>7</sub> β-barrel domain</scene>. The <scene name='77/775266/Cv/12'>active site</scene> of the enzyme is found between these two domains<ref>PMID:179444491</ref>. Water molecules are shown as red spheres. <scene name='77/775266/Cv/13'>Mg coordination site</scene>.
 </StructureSection>