Beta-ketoacyl-ACP reductase
From Proteopedia
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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. | 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. | ||
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| + | ==3D structures of beta-ketoacyl carrier protein reductase== | ||
| + | [[Beta-ketoacyl carrier protein reductase 3D structures]] | ||
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</StructureSection> | </StructureSection> | ||
Revision as of 07:54, 11 April 2019
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3D structures of beta-ketoacyl carrier protein reductase
Updated on 11-April-2019
References
- ↑ 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
