2.7.2.8	?	x * 52000, SDS-PAGE	390290	
2.7.2.8	?	x * 29000, SDS-PAGE	642355	
2.7.2.8	additional information	due to the capacity for self-association the enzyme can exist in different states of aggregation depending on the nature of the ligands and the concentration of phosphate buffer	642355	
2.7.2.8	?	dimer or tetramer, 1 or 2 * 43000 + 1 or 2 * 53000, SDS-PAGE	642358	
2.7.2.8	dimer	2 * 30000, SDS-PAGE	642361	
2.7.2.8	dimer	crystalline structure	642363	
2.7.2.8	hexamer	6 * 30341, MALDI-TOF MS, 6 * 30344, calculated	659050	
2.7.2.8	hexamer	6 * 32000, calculated	659433	
2.7.2.8	additional information	enzyme hexamer forms a complex with PII signaling protein trimer	659433	
2.7.2.8	additional information	in vivo complex of enzyme with signal transduction protein PII	659433	
2.7.2.8	additional information	possible interaction of enzyme with PII signal proteins in vivo	660146	
2.7.2.8	hexamer	three homodimers are linked to form a ring-like hexamer	675366	
2.7.2.8	monomer	-	689895	
2.7.2.8	hexamer	with an extra N-terminal-linked helix interlinking three dimers, the hexameric architecture is not essential for arginine inhibition but is functionally essential for physiologically relevant arginine control of NAGK	692856	
2.7.2.8	hexamer	-	-, 702066, 760403	
2.7.2.8	tetramer	crystal structure	720845	
2.7.2.8	homodimer	-	722965	
2.7.2.8	dimer	-	723511	
2.7.2.8	tetramer	-	723557	
2.7.2.8	homodimer	2 * 27000, SDS-PAGE	760403