1.1.1.45	dimer	2 * 35000	669147	
1.1.1.45	dimer	2 * 36000, recombinant enzyme, SDS-PAGE	712765	
1.1.1.45	dimer	alpha2, 2 * 33000-35000, SDS-PAGE	286911	
1.1.1.45	dimer	alphabeta, 1 * 23500 + 1 * 40000, SDS-PAGE	286910	
1.1.1.45	monomer	X-ray diffraction, natural active protein is presumably a dimer 2 * 36000	695345	
1.1.1.45	additional information	the enzyme possesses two domains, the N-terminal domain with a Rossmann fold and the C-terminal domain with a helical fold. In the N-terminal domain of the NADH-bound structure exist 11 coenzyme-binding residues and two distinct side-chain conformers of coenzyme binding residue Ser124. Subunit dimerization is mediated by numerous intersubunit interactions, including 22 hydrogen bonds and 104 residue pairs of van der Waals interactions, of which those between two cognate C-terminal domains are predominant. Domain and subunit interface structures, structure comparison with the human enzyme, overview	712765