ATP-citrate synthase

spinqualitylabelsall models ATP-citrate synthase complex with ADP (stick model), tartrate and Mg+2 ions (green), 3pff Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function ATP-citrate synthase (ACS) is part of the citrate cycle. It catalyzes the transformation of ADP, acetyl-CoA and oxaloacetate to ATP, citrate and CoA. ACS is the link between energy metabolism from carbohydrates to the production of fatty acids. See also Citrate Synthase Structural highlights Crystal structures have shown that tartrate and citrate bind to ACS in the same binding site. Binding site of tartrate of ATP-citrate synthase. Water molecules are shown as red spheres. Binding site of ADP and Mg+2 ions, 3pff. 3D Structures of ATP-citrate synthase ATP-citrate synthase 3D structures

3D Structures of ATP-citrate synthase

Updated on 25-March-2019

Citrate Synthase, 3pff – hACS + citrate – human
ATP-citrate synthase 3D structures, 5tet – hACS + citrate derivative
5teq – hACS N-terminal (mutant) + citrate
5te1 – hACS N-terminal (mutant) + citrate derivative
5tes – hACS + citrate + ADP
5tdm – hACS + citrate derivative + ADP
3mwe – hACS + tartrate
3pff, 5tdz - hACS + tartrate + ADP

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