3.5.4.B9	dimer	-	721668, 723256	
3.5.4.B9	monomer or dimer	x * 46000, the enzyme is active in monomeric, dimeric, and larger oligomeric states	722665	
3.5.4.B9	additional information	A3G contains two cytidine deaminase domains. The CD2 domain possesses the deamination activity	721103	
3.5.4.B9	additional information	Apo3G has a catalytically inactive N-terminal CD1 domain and an active C-terminal CD2 domain. Apo3G exists as monomers, dimers, tetramers, and higher order oligomers whose distributions depend on DNA substrate and salt	712428	
3.5.4.B9	additional information	APOBEC3G cytidine deaminase catalytically inactive N-terminal CD1 domain has a predicted large net positive charge, in contrast to the catalytically active CD2 domain, and is likely to govern the mobility of APOBEC3G cytidine deaminase on ssDNA, which should depend on metal ion concentration	720014	
3.5.4.B9	additional information	the enzyme is a mix of monomers, dimers, and higher order oligomers	721999