3.5.1.42	dimer	an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state	-, 734285	
3.5.1.42	homodimer	2 * 19000, recombinant enzyme, SDS-PAGE	-, 755141	
3.5.1.42	homodimer	2 * 47000, SDS-PAGE	719984	
3.5.1.42	homodimer	2 * 47320, recombinant His6-tagged enzyme, mass spectrometry	-, 735110	
3.5.1.42	homodimer	2 * about 20000, SDS-PAGE	719984	
3.5.1.42	additional information	enzyme structure comparisons	733870	
3.5.1.42	oligomer	heat-stable and heat-sensitive subunits	209139