EC Number   |
Subunits |
Reference |
|---|
    1.1.1.3 | homodimer |
2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE |
-, 741408 |
| 1.1.1.3 | dimer |
2 * 38000, SDS-PAGE, threonine resistant isozyme |
246385 |
| 1.1.1.3 | dimer |
2 * 40000, SDS-PAGE |
246399 |
| 1.1.1.3 | dimer |
2 * 40600, calculated, 2 * 40000, SDS-PAGE |
712490 |
| 1.1.1.3 | dimer |
2 * 55000, SDS-PAGE |
246389 |
| 1.1.1.3 | tetramer |
4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE |
-, 761687 |
| 1.1.1.3 | tetramer |
4 * 55000, SDS-PAGE |
246395 |
| 1.1.1.3 | dimer |
crystal structure |
246396 |
| 1.1.1.3 | homodimer |
dimeric enzyme structure, overview |
-, 739972 |
| 1.1.1.3 | More |
enzyme TtHSD folds into a dimer with a noncrystallographic 2fold axis. The subunit comprises three conserved domains of HSDs and a flexible tail at the C-terminus. The nucleotide-binding domain (residues 1-119 and 288-309) assumes an alpha/beta Rossmann fold with five beta-strands and four alpha-helices. The dimerization domain (residues 120-140 and 261-287) comprises two alpha-helices and two beta-strands that interact with the corresponding domain of the other subunit of the dimer to form an alpha/beta structure with the four-stranded beta-sheet. The substrate-binding domain (residues 141-260) comprises four beta-strands and five alpha-helices. The flexible tail at the C-terminus (310-332) extends from the nucleotide-binding domain to the substrate-binding domain |
761404 |
