1.1.1.282	dimer	-	-, 644536, 739956	
1.1.1.282	dimer	2 * 31350, wild type enzyme, gel filtration	656292	
1.1.1.282	dimer	distinct mode of dimerization in which the individual molecules interact in a back-to-front manner, overview. The molecules of the RifI2 dimer associate via hydrophobic interactions between residues on alpha-helix alpha8 of the first molecule and alpha10' of the second molecule. In addition, the side chain of Gln167 on apha-helix alpha8 forms a hydrogen bond with the guanidinium group of Arg243' on beta-strand beta10'. A second hydrogen bond to Arg243' may be made by Asn171. Asp53 and Arg56 on alpha-helix alpha2 bind the imidazole ring of His31' on alpha-helix alpha1'	-, 740100	
1.1.1.282	homodimer	-	644537	
1.1.1.282	homodimer	2 * 30000, about, recombinant enzyme, SDS-PAGE	-, 724089	
1.1.1.282	monomer	1 * 31500, SDS-PAGE	-, 654384	
1.1.1.282	monomer	1 * 41000	286356	
1.1.1.282	additional information	enzyme three-dimensional structure determination, analysis, and comparisons, overview. The N-terminal or catalytic domain comprises residues 1 to 113 and 256 to 283, whereas the C-terminal or nucleotide-binding domain is build up of residues 114 to 255. The catalytic domain forms an open alpha/beta sandwich, which is characteristic for enzymes of the SDH/QDH family. The substrate-binding site is located in the N-terminal domain, close to the nicotinamide ring of the cofactor	-, 727115