5.3.3.17	dimer	2 * 32218, histidine-tagged enzyme	-, 702206	
5.3.3.17	dimer	deduced from crystal structure. The crystal structure clarifies that the enzyme is a dimer in an up/up configuration with the two active sites facing each other. The dimer in the open form, generates by crystal symmetry (sulfate complex), interacts mainly through the alpha1-helices and the beta16-strands in the N-terminal domains. The C-terminal domains are not in direct contact but are relatively close	706479	
5.3.3.17	homodimer	-	749064