EC Number   |
Cofactor |
Reference |
|---|
    1.4.3.2 | FAD |
- |
391766, 391815, 391823, 668580, 669658, 669894, 670963, 690693, 692288, 695281, 711329, 711786, 713525, 713558, 713559, 724190, 724397, 724486, 724814, 724964, 725027, 725575, 726320, 726520, 726521, 741725, 741736, 741737, 741749, 742047, 742530, 742690, 742813, 742930, 743253, 743871, 743872, 762657, 762771, 763414, 763758 |
| 1.4.3.2 | FAD |
1 mol of FAD per mol of enzyme |
391808 |
| 1.4.3.2 | FAD |
2 mol of FAD per mol of enzyme |
389803, 391766, 391770, 391772, 391774, 391824 |
| 1.4.3.2 | FAD |
4 mol of FAD per mol of enzyme |
391787 |
| 1.4.3.2 | FAD |
a flavoenzyme |
696493 |
| 1.4.3.2 | FAD |
a homodimer complex containing 2 FAD molecules |
651026 |
| 1.4.3.2 | FAD |
FAD loading of the enzyme expressed in Pichia pastoris is 80%-100% in different expressions |
763454 |
| 1.4.3.2 | FAD |
non-covalently bound |
391814, 667079, 695361 |
| 1.4.3.2 | FAD |
the FAD-binding domain includes residues 35-72, 239-318 and 446-486. The secondary structure elements of this domain are 4 alpha-helices |
712998 |
| 1.4.3.2 | FAD |
the whole cofactor is buried inside the protein and is not solvent accessible. The FAD-binding domain consists of three discontinuous regions of the structure: residues 4-51, 239-314 and 423-488. The main structural feature of this domain is a fivestranded beta-pleated sheet sandwiched between three alpha-helices and a four-stranded beta-pleated sheet. The FAD-binding domain corresponds to a general topology throughout the whole GR2-famil |
669894 |
