EC Number   |
Cofactor |
Reference |
|---|
   1.18.1.2 | 2Fe-2S-center |
- |
674373 |
| 1.18.1.2 | FAD |
- |
285496, 285502, 285524, 285530, 285540, 285546, 285548, 657696, 657970, 658208, 659483, 660140, 674373, 685270, 685845, 714174, 716444, 716461, 716851, 727243, 739253, 743411, 743415, 743418, 745371, 745988, 745997, 746132 |
| 1.18.1.2 | FAD |
0.98 mol FAD tightly bound to 1 mol of enzyme |
658608 |
| 1.18.1.2 | FAD |
1 mol FAD per mol of enzyme |
285475, 285519 |
| 1.18.1.2 | FAD |
48% FAD semiquinone at the equilibrium, pH 7.0 |
671585 |
| 1.18.1.2 | FAD |
a-FAD and b-FAD, binding of FAD and the iron-sulfur clusters in the NfnAB complex, overview |
742880 |
| 1.18.1.2 | FAD |
and FMN, ratio of FAD to FMN is 7.5 to 1 |
721789 |
| 1.18.1.2 | FAD |
binding and hydride/electron transfer mechanism |
658076 |
| 1.18.1.2 | FAD |
binding domain structure, structure-function relationship |
660066 |
| 1.18.1.2 | FAD |
BsFNR features two distinct binding domains for FAD and NADPH, binding structure, overview. A unique C-terminal extension covers the re-face of the isoalloxazine moiety of FAD. Tyr50 in the FAD-binding region and His324 in the Cterminal extension stack on the si- and re-faces of the isoalloxazine ring of FAD, respectively |
716852 |
