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Acyl-CoA dehydrogenase

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SCAD is a homodimer with a single FAD binding site. <scene name='49/491924/Cv/2'>MCAD is a homotetramer</scene> with <scene name='49/491924/Cv/3'>4 FAD binding sites in the subunits interface and 4 binding sites for acyl-CoA substrate within each monomer</scene>.
SCAD is a homodimer with a single FAD binding site. <scene name='49/491924/Cv/2'>MCAD is a homotetramer</scene> with <scene name='49/491924/Cv/3'>4 FAD binding sites in the subunits interface and 4 binding sites for acyl-CoA substrate within each monomer</scene>.
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*<scene name='49/491924/Cv/4'>FAD binding site</scene>.
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*One of the <scene name='49/491924/Cv/4'>FAD binding sites</scene>.
</StructureSection>
</StructureSection>
==3D structures of acyl-CoA dehydrogenase==
==3D structures of acyl-CoA dehydrogenase==

Revision as of 15:22, 3 December 2015

Rat short chain acyl-CoA hydrogenase dimer complex with cofactor FAD and CoA (PDB code 1jqi)

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3D structures of acyl-CoA dehydrogenase

Updated on 03-December-2015

References

  1. ↑ Thorpe C, Kim JJ. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 1995 Jun;9(9):718-25. PMID:7601336

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