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Fig. 1 | Lipids in Health and Disease

Fig. 1

From: Characterization of two ETFDH mutations in a novel case of riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency

Fig. 1

Schematic representation of ETFDH structural domains. ETFDH protein (amino acids 1–617) has three functional regions: the 4Fe4S cluster (amino acids C4-Y16 and D484-M584; the FAD-binding domain (amino acids P17-N106, V141-P235 and S340-V418), that contains in the first segment, between G42-G47 residues, an ADP-binding motif; the UQ-binding domain (amino acids T107-V140, Q236-Q339 and S417-F483). Furthermore, two membrane-binding surface regions are located in the UQ domain

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