Phosphoglycerate Kinase: Difference between revisions
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PGK structure shows an open-to-close transition upon hinge bending. PG assumes the open conformation upon release of PGA and ATP. The closed conformation active site contains PGA, ADP and AlF<sub>4</sub>-1 ion which mimics the phosphate ion<ref>PMID:21549713</ref>. | PGK structure shows an open-to-close transition upon hinge bending. PG assumes the open conformation upon release of PGA and ATP. The closed conformation active site contains PGA, ADP and AlF<sub>4</sub>-1 ion which mimics the phosphate ion<ref>PMID:21549713</ref>. | ||
*<scene name='38/387911/Cv/ | *<scene name='38/387911/Cv/10'>Phosphoglycerate binding site</scene>. | ||
*<scene name='38/387911/Cv/ | *<scene name='38/387911/Cv/11'>AlF4- binding site</scene>. | ||
*<scene name='38/387911/Cv/ | *<scene name='38/387911/Cv/12'>ADP binding site</scene>. | ||
*<scene name='38/387911/Cv/ | *<scene name='38/387911/Cv/13'>Whole binding site</scene>. Water molecules are shown as red spheres. | ||
== Reaction Mechanism == | == Reaction Mechanism == | ||