1.17.4.2	dimer	-	437893	
1.17.4.2	dimer	both subunits are required for catalytic activity	715583	
1.17.4.2	monomer	-	437889, 437892, 437893, 437895, 437896	
1.17.4.2	monomer	1 * 50000, SDS-PAGE	-, 437893	
1.17.4.2	monomer	1 * 76000	714186	
1.17.4.2	monomer	1 * 78400, SDS-PAGE	437890	
1.17.4.2	monomer or dimer	alpha or alpha2, class II RNRs	715085	
1.17.4.2	monomer or dimer	class II enzymes show a monomeric or dimeric structure	716317	
1.17.4.2	additional information	structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview	715085	
1.17.4.2	additional information	structures of the active holoenzymes of class I-III RNRs, structure comparisons, overview	716317	
1.17.4.2	additional information	the enzyme is encoded by two consecutive open reading frames denated nrdJa and nrdJb and separated by 16 bp. The presence of both NrdJa and NrdJb subunits is absolutely essential for enzyme activity	659464	
1.17.4.2	tetramer	2 * M1-subunit + 2 * M2-subunit	688754	
1.17.4.2	tetramer	4 * 100000, SDS-PAGE	-, 437891	
1.17.4.2	tetramer	alpha2beta2 heterodimer with a regulatory, nucleotide binding site M1 subunit, and an inducible, catalytic M2 subunit which contains non-heme iron and a tyrosyl free radical, that are required for the enzymatic reduction of ribonucleotides	688750	
1.17.4.2	tetramer	alpha2beta2, class III RNRs	715085	
1.17.4.2	tetramer	RNR is a tetramer consisting of two non-identical homodimers. The two identical M2 subunits regulate the substrate specificity of the enzyme, while the other two identical M1 subunits are responsible for the activity by binding the ribonucleotides and allosteric effectors	685023