Beta-ketoacyl-ACP reductase

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== Structural highlights ==
== Structural highlights ==
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The <scene name='59/593279/Cv/2'>active site</scene> interacting with co-factor NADPH contains the active site catalytic triad <scene name='59/593279/Cv/3'>S138, Y151, K155</scene> (in E. coli, PDB code [[1q7b]]).<ref>PMID:15016358</ref>
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The <scene name='59/593279/Cv/4'>active site</scene> interacting with co-factor NADPH contains the active site catalytic triad <scene name='59/593279/Cv/5'>S138, Y151, K155</scene> (in E. coli, PDB code [[1q7b]]).<ref>PMID:15016358</ref> Water molecules are shown as red spheres.
</StructureSection>
</StructureSection>

Revision as of 11:07, 23 May 2018

Structure of beta-ketoacyl carrier protein reductase complex with NADP and Ca+2 ion (green) (PDB code 1q7b).

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3D structures of beta-ketoacyl carrier protein reductase

Updated on 23-May-2018


References

  1. Price AC, Zhang YM, Rock CO, White SW. Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG. Structure. 2004 Mar;12(3):417-28. PMID:15016358 doi:10.1016/j.str.2004.02.008

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