1.14.14.3	heterodimer	alphabeta, 1 * 41389 + 1 * 37112, nucleotide sequence	348543	
1.14.14.3	heterodimer	-	348548, 348597, 348599, 348600, 348601	
1.14.14.3	monomer	1 * 78000, produced by gene fusion of luxA and luxB genes	348549	
1.14.14.3	heterodimer	alphabeta, 1 * 40108 + 1 * 36349 nucleotide sequence	348565, 348566	
1.14.14.3	additional information	functional roles of conserved residues in the protease-labile, unstructured loop of the alpha-subunit, formed by residues 257-291, the loop undergoed conformational changes during catalysis, overview	657923	
1.14.14.3	additional information	analysis of subunit interface structure and role in the conformational stability of the heterodimeric enzyme, the beta-sunbunit can self-associate to form a stable but inactive homodimer, unfolding in a four-state mechanism	657927	
1.14.14.3	additional information	structure-function relationship, roles of Cys106, Ala75, Ala74, and the isoalloxazine ring of FMN	657939	
1.14.14.3	dimer	heterodimer	658060	
1.14.14.3	dimer	alphabeta heterodimer containing a single active site at a cleft in the alpha subunit	671978	
1.14.14.3	dimer	alphabeta heterodimer, structure-function relationship, overview	671985	
1.14.14.3	heterodimer	alpha-subunit, encoded by the luxA gene, and beta-subunit, encoded by the luxB gene	-, 711341	
1.14.14.3	additional information	luciferase is composed of two homologous subunits designated alpha and beta, both of which assume the TIM barrel fold. Although the beta-subunit is required for activity, the catalytic site resides exclusively on the alpha-subunit. The most substantial compositional difference between subunits corresponds to a highly conserved stretch of residues between positions 260 and 290 unique to the alpha chains of luminous bacteria. In the luciferase/FMN complex, the asymmetric unit contains two beta/alpha-heterodimers	711486	
1.14.14.3	homodimer	2 * 77000, SDS-PAGE	728017	
1.14.14.3	homodimer	2 * 77800, calculated from amino acid sequence	728017