Beta-ketoacyl-ACP reductase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | 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]]). | + | 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> |
</StructureSection> | </StructureSection> | ||
Revision as of 09:03, 16 November 2015
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3D structures of beta-ketoacyl carrier protein reductase
Updated on 16-November-2015
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
