1.1.1.95	?	x * 47700, calculated from amino acid sequence	-, 739236	
1.1.1.95	?	x * 50000, SDS-PAGE	-, 739236	
1.1.1.95	?	x * 55000, SDS-PAGE	656277	
1.1.1.95	?	x * 57000, SDS-PAGE	700437	
1.1.1.95	?	x * 59000, SDS-PAGE	-, 737455	
1.1.1.95	?	x * 66453 and 90000, DNA sequence analysis and SDS-PAGE	287549	
1.1.1.95	dimer	-	-, 726890, 763528	
1.1.1.95	dimer	2 * 33500, calculation from nucleotide sequence	655484	
1.1.1.95	dimer	mutant enzyme SerADELTA197	654296	
1.1.1.95	homodimer	2 * 35000 at pH 7.0	725917	
1.1.1.95	homodimer	2 * 35000, SDS-PAGE	738401	
1.1.1.95	homodimer	gel filtration	684698	
1.1.1.95	homodimer	x-ray crystallography	738215	
1.1.1.95	homooctamer	8 * 60000, SDS-PAGE, AtPGDH2 forms an equilibrium of homooctamers and homotetramers	763716	
1.1.1.95	homotetramer	4 * 55000, calculated from amino acid sequence	737556	
1.1.1.95	homotetramer	4 * 56800	698189	
1.1.1.95	homotetramer	4 * 57200, calculated from amino acid sequence	737556	
1.1.1.95	homotetramer	4 * 60000, SDS-PAGE	763108, 763716	
1.1.1.95	homotetramer	4 * 60000, SDS-PAGE, AtPGDH2 forms an equilibrium of homooctamers and homotetramers	763716	
1.1.1.95	monomer	1 * 35000 at pH 5.0	725917	
1.1.1.95	additional information	each subunit consists of three distinct domains: a cofactor or nucleotide binding domain, a substrate binding domain, and a regulatory domain. Structural molecular modeling of mutant enzymes, overview	698189	
1.1.1.95	additional information	quarternary structure of the active enzyme, conformational changes through domain-domain reorientation, stereochemical model, overview	667663	
1.1.1.95	additional information	subunit structure with substrate binding domain, coenzyme binding domain and regulatory domain, active sites	287547, 287550, 287551	
1.1.1.95	additional information	the apo-enzyme shows an extreme asymmetry in the orientation of the domains from one subunit to another. The poly glycine stretch in the loop that contains the locus for the 160° rotation leads to subunit asymmetry, structure modelling, overview	-, 696285	
1.1.1.95	additional information	the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism	663605	
1.1.1.95	additional information	the enzyme contains an ACT regulatory domain, enzyme domain structure	667649	
1.1.1.95	tetramer	4 * 40000-43000, SDS-PAGE, sedimentation equilibrium studies in guanidine hydrochloride	287544	
1.1.1.95	tetramer	4 * 40000-50000, sedimentation equilibrium in guanidine-HCl	287530	
1.1.1.95	tetramer	4 * 44000, SDS-PAGE, each subunit is divided into 3 separate domains	287545, 287547	
1.1.1.95	tetramer	4 * 60000, SDS-PAGE	287539	
1.1.1.95	tetramer	although the tetramer is composed of identical subunits, significant asymmetry is seen in the tertiary structure of the subunits	656278	
1.1.1.95	tetramer	gel filtration	687641	
1.1.1.95	tetramer	intervening domains are the two four-stranded beta-sheet structures located next to the substrate binding domains and below the regulatory domains, structure model, overview	-, 696336	
1.1.1.95	tetramer	ligand-bound enzyme, sequence comparison	-, 696285	
1.1.1.95	tetramer	wild-type enzyme	654296