3.4.21.B30	?	x * 24000, recombinant enzyme variant UmuDAb, SDS-PAGE	731823	
3.4.21.B30	dimer	2 * 15063	668783	
3.4.21.B30	dimer	although UmuD and UmuD' form homodimers, they preferentially form heterodimers, crosslinking experiments, SDS-PAGE	653604	
3.4.21.B30	dimer	although UmuD and UmuD' form homodimers, they preferentially form heterodimers, SDS-PAGE	650976	
3.4.21.B30	dimer	crystallization experiments	653917	
3.4.21.B30	dimer	enzyme can form homodimers, crosslinking experiments, SDS-PAGE	651622, 651630	
3.4.21.B30	dimer	UmuD and the cleavage product UmuD' exist as homodimers. Their subunits can readily exchange to form UmuDD' heterodimers preferentially. Heterodimer formation is an essential step in the degradation pathway of UmuD'	-, 752775	
3.4.21.B30	dimer	UmuD can form homodimers, crosslinking experiments, SDS-PAGE	651628	
3.4.21.B30	dimer	UmuD dimers exchange readily, and the subunits of UmuD2 and UmuD'2 exchange to form the UmuDD' heterodimer. The heterodimer is the preferred but not exclusive protein form, and both the heterodimer and homodimers exhibit slow exchange kinetics, which is further inhibited in the presence of interacting partner DinB	-, 731345	
3.4.21.B30	heterodimer	UmuD and UmuD’ rapidly form heterodimers in vitro	717851	
3.4.21.B30	homodimer	-	718023	
3.4.21.B30	homodimer	2 * 15000, recombinant enzyme UmuD, SDS-PAGE	731823	
3.4.21.B30	homodimer	2 * 15500, predicted from amino acid sequence	682581	
3.4.21.B30	homodimer	UmuD2	709543, 718102	
3.4.21.B30	additional information	in addition to forming molecular dimers, the N-and C-terminal tails of UmuD' extend from a globular beta structure to associate and produce crystallized filaments. Higher oligomers are found in solution with UmuD' but not with UmuD nor with a mutant of UmuD' lacking the extended N terminus	653917	
3.4.21.B30	additional information	UmuD proteins are shown to adopt multiple conformations in solution. UmuD contains only one cysteine (residue 24) per monomer at the cleavage site, which is between residues C24 and G25, cleavage of UmuD to form UmuD? removes the N-terminal 24 amino acids, which includes residue C24	-, 731345	
3.4.21.B30	tetramer	two dimers form a tetramer, wild-type and V34C mutant, SDS-PAGE	651628