Group:SMART:2010 Pingry SMART Team: Difference between revisions
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'''Design description''' | '''Design description''' | ||
The conformation of 2.5-DKGR A is a parallel alpha/beta barrel of eight <scene name='2010_Pingry_SMART_Team/1a80-default/2'>alpha helices(highlighted red) and eight beta strands(highlighted blue).</scene> Notably, the alpha-beta 8 structure is common among other enzymes of the aldo-keto reductase family. Located at the C-terminal side of the barrel is the active site for the NADPH cofactor to bind to 2.5-DKGR A. | The conformation of 2.5-DKGR A is a parallel alpha/beta barrel of eight <scene name='2010_Pingry_SMART_Team/1a80-default/2'>alpha helices(highlighted red) and eight beta strands(highlighted blue).</scene> Notably, the alpha-beta 8 structure is common among other enzymes of the aldo-keto reductase family. Located at the C-terminal side of the barrel is the active site for the | ||
<scene name='2010_Pingry_SMART_Team/1a80-original/12'>NADPH cofactor(shown in wireframe and colored CPK)</scene> to bind to 2.5-DKGR A. | |||
<scene name='2010_Pingry_SMART_Team/1a80-default/1'>(Lys232, Phe22, Arg238, Ala272).</scene> | <scene name='2010_Pingry_SMART_Team/1a80-default/1'>(Lys232, Phe22, Arg238, Ala272).</scene> | ||
