3.1.8.2	?	x * 34000, SDS-PAGE	664937	
3.1.8.2	?	x * 34000, SMP30, SDS-PAGE	664937	
3.1.8.2	?	x * 35000	713615	
3.1.8.2	?	x * 35000, SDS-PAGE	752291, 755573	
3.1.8.2	?	x * 45000, about, SDS-PAGE	749628	
3.1.8.2	?	x * 56847, wild-type enzyme, sequence calculation, x * 55000, recombinant wild-type enzyme, SDS-PAGE, x * 77000, recombinant engineered His-tagged InaV-N-DFPase enzyme, SDS-PAGE	749614	
3.1.8.2	?	x * 58000, the enzyme OPAA structure is composed of two domains, a small N-terminal domain or N-domain, residue 1 to 160, and a large C-terminal domain or C-domain	-, 707530	
3.1.8.2	?	x * 58500	714729	
3.1.8.2	?	x * 73000, SDS-PAGE	670953	
3.1.8.2	homodimer	2 * 35000, OPH from displays the TIM barrel fold in the active site loaded with Zn2+, overview	713896	
3.1.8.2	monomer	1 * 53000 SDS-PAGE	646548	
3.1.8.2	monomer	1 * 60000, SDS-PAGE, under reducing and nonreducing conditions	646547	
3.1.8.2	additional information	features observed in the structure of PON1, i.e. the six-bladed beta-propeller scaffold, the three alpha-helices at the top of the propeller and the putative calcium-binding residues, are well conserved in the modelled structures	749628	
3.1.8.2	additional information	the molecular conformation of DFPase is similar to other phosphotriesterases such as paraoxonase 1 (PON1, EC 3.1.8.1)	750923	
3.1.8.2	tetramer	active enzyme	713896	
3.1.8.2	tetramer	active enzyme, OPAA/prolidase from Alteromonas sp. JD6.5 displays the pita bread fold in the C-terminal region which houses the active metal site loaded with Mn2+, overview	-, 713896