5.4.2.11	?	x * 30000, SDS-PAGE	748279	
5.4.2.11	dimer	-	3240	
5.4.2.11	dimer	2 * 21948, calculated	660633	
5.4.2.11	dimer	2 * 28000-28600, SDS-PAGE	3254, 3255	
5.4.2.11	dimer	2 * 29000, SDS-PAGE	3248	
5.4.2.11	dimer	2 * 29000, SDS-PAGE, immunologically the MM-type and BB-type subunits show cross-reactivity as shown by ELISA and immunological neutralization, evidence for common antigenic determinants	3236	
5.4.2.11	dimer	crystal structure	652877	
5.4.2.11	homotetramer	2 * 26000, calculated from amino acid sequence	-, 715964	
5.4.2.11	monomer	1 * 23700	652846	
5.4.2.11	additional information	heterodimer structure of phosphoglycerate mutase/bisphosphoglycerate mutase crystallization data	660903	
5.4.2.11	additional information	molecular dynamics simulation reveals that the enzyme interacts with its C-terminal domain with enolase, suggesting a direct transfer mechanism of substrate	680944	
5.4.2.11	tetramer	4 * 23678, chromosomal enzyme, 4 * 23669, mutants H196Q and H151Q, 4 * 23668, mutant H163Q, mass spectrometry	3221	
5.4.2.11	tetramer	4 * 27000, SDS-PAGE	649656	
5.4.2.11	tetramer	4 * 28000, SDS-PAGE	3229	
5.4.2.11	tetramer	crystal structure	3216	
5.4.2.11	tetramer	identical subunits of 4 * 246 amino acids	3216