Mandelate racemase/muconate lactonizing enzyme
From Proteopedia
(Difference between revisions)
												
			
			| Line 7: | Line 7: | ||
== Structural highlights ==  | == Structural highlights ==  | ||
| - | 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   | + | 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
  | |||||||||||
3D Structures of Mandelate racemase/muconate lactonizing enzyme
Updated on 06-December-2017

