EC Number   |
Subunits  |
Reference |
|---|
    1.1.1.3 | homodimer |
2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE |
-, 741408 |
| 1.1.1.3 | homodimer |
dimeric enzyme structure, overview |
-, 739972 |
| 1.1.1.3 | homodimer |
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview |
-, 739791 |
| 1.1.1.3 | homopentamer or homohexamer |
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation |
-, 760736 |
| 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 |
| 1.1.1.3 | More |
primary and secondary structure comparison, the bifunctional enzyme contains 2 homologous subdomains defined by a common loop-alpha helix-loop-beta strand-loop-beta strand motif, the enzymes' regulatory domain is composed of 2 subdomains, amino acid residues 414-453 and 495-534 |
642341 |
| 1.1.1.3 | More |
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview |
-, 739791 |
| 1.1.1.3 | More |
structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview |
-, 740548 |
| 1.1.1.3 | More |
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs |
-, 761687 |
| 1.1.1.3 | tetramer |
4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE |
-, 761687 |
