1.1.1.3	?	x * 85000, SDS-PAGE, threonine sensitive isozyme	246383	
1.1.1.3	dimer	2 * 38000, SDS-PAGE, threonine resistant isozyme	246385	
1.1.1.3	dimer	x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme	246385	
1.1.1.3	tetramer	x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme	246385	
1.1.1.3	dimer	2 * 55000, SDS-PAGE	246389	
1.1.1.3	tetramer	4 * 55000, SDS-PAGE	246395	
1.1.1.3	dimer	crystal structure	246396	
1.1.1.3	dimer	2 * 40000, SDS-PAGE	246399	
1.1.1.3	hexamer	in absence of L-threonine	642340	
1.1.1.3	tetramer	in presence of L-threonine	642340	
1.1.1.3	additional information	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	dimer	2 * 40600, calculated, 2 * 40000, SDS-PAGE	712490	
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	additional information	structural basis for the catalytic mechanism of homoserine dehydrogenase, overview	-, 739791	
1.1.1.3	homodimer	dimeric enzyme structure, overview	-, 739972	
1.1.1.3	additional information	structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview	-, 740548	
1.1.1.3	homodimer	2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE	-, 741408	
1.1.1.3	homopentamer or homohexamer	x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation	-, 760736	
1.1.1.3	?	x * 35492, sequence calculation	761404	
1.1.1.3	additional information	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	additional information	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	
1.1.1.3	dimer	StHSD is composed of a nucleotide-binding region (residues 1-130 and 285-304), a dimerization region (residues 131-145 and 256-284), and a catalytic region (residues 146-255). Presence of a disulfide bond formed between two cysteine residues (position 304) in the C-terminal regions of the two subunits	-, 762453