Oxidoreductase FAD-binding domain
From Wikipedia, the free encyclopedia
| Oxidoreductase FAD-binding domain | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | FAD_binding_6 | ||||||||||
| Pfam | PF00970 | ||||||||||
| InterPro | IPR008333 | ||||||||||
| SCOP2 | 1cne / SCOPe / SUPFAM | ||||||||||
| CDD | cd00322 | ||||||||||
| |||||||||||
The oxidoreductase FAD-binding domain is an evolutionary conserved protein domain. To date, the 3D-structures of the flavoprotein domain of Zea mays nitrate reductase[1] and of pig NADH:cytochrome b5 reductase[2] have been solved. The overall fold is similar to that of ferredoxin:NADP+ reductase:[3] the FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel, while the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet flanked by 2 helices on each side).