EC Number   |
Subunits |
Reference |
|---|
   1.5.1.39 | dimer |
flavin-bound wild-type enzyme, and enzyme mutant Y118A and DELTAY118 |
765724 |
| 1.5.1.39 | monomer |
1 * 42000, recombinant His-tagged enzyme, SDS-PAGE |
-, 764601 |
| 1.5.1.39 | monomer |
ChuY exists as a monomer in solution, SDS-PAGE and gel filtration |
-, 741831 |
| 1.5.1.39 | More |
the conserved protein fold of LrFOR is comprised of about eight alpha-helices and eight parallel beta-strands that alternate along the peptide backbones (A (beta/alpha) 8 barrel) |
-, 764601 |
| 1.5.1.39 | More |
the tetramer of enzyme SsuE binds FMN, and dissociates to a dimer. In a flavin-bound SsuE structure, the hydroxyl group of Tyr118 hydrogen bonds to the oxygen atom backbone carbonyl of Ala78 across the tetramer interface |
765724 |
| 1.5.1.39 | More |
the two molecules in the asymmetric unit are related by pseudo 2fold rotation symmetry. ChuY contains six alpha-helices and ten beta-strands. A central beta-sheet, consisting of seven parallel beta-strands, beta1, beta2, beta3, beta4, beta5, beta6, and beta10, is flanked by six alpha-helices, forming alternating beta-strand and alpha-helix repeats, which is a representative feature of Rossmann folds. Three other beta-strands (beta7-beta9) are located on the top of the beta-sheet |
-, 741831 |
| 1.5.1.39 | tetramer |
flavin-free wild-type enzyme |
765724 |
