Isocitrate dehydrogenase: Difference between revisions

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 Isocitrate dehydrogenase is SCOP classified as an alpha beta structure. Its secondary composition consists of mainly alpha helices and beta sheets which are arranged into three layer alpha beta alpha sandwich structures. The entire protein consists of two side by side sandwich structures that face opposite directions. This then causes the proteins two active sites to face opposite directions. These two groups make up the A and B subunits of isocitrate dehydrogenase.
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 {{STRUCTURE_1to9 |  PDB=3cin  |  SCENE=  }}
+=='''The Active Site'''==
+The active site of Isocitrate dehydrogenase binds the NAD+ or an NADP+ molecule as well as an Mg+ or Ca2+. This metal ion seems to be essential for catalysis<ref>PMID:15173171.</ref>. Side chains of Asp 279 form hydrogen bonds with Ser94 (Human isocitrate dehydrogenase). Isocitrate is able to bind to the active site using about 8 amino acids like tyrosine, serine, asparagine, arginine, arginine, arginine, tyrosine, and lysine<ref>PMID:17632124.</ref>. Across species these are not perfectly conserved by they are replaced with residues of