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EC Number	Subunits	Commentary	Reference
1.13.11.24	?	x * 23041, calculated from sequence	-, 684750
1.13.11.24	?	x * 37640, MALDI-TOF, SDS-PAGE	657272
1.13.11.24	dimer	crystallization data	654768
1.13.11.24	dimer	SDS-PAGE	-, 702220
1.13.11.24	dimer	the enzyme is a dimer of monocupin subunits	742192
1.13.11.24	homodimer	bicupin domain structure	724015
1.13.11.24	homodimer	bicupin enzyme	725130
1.13.11.24	homodimer	he enzyme forms homodimers, which are stabilized by an N-linked heptasaccharide at the dimer interface. The mononuclear type 2 copper center displays two distinct geometries: a distorted tetrahedral coordination, formed by His66, His68, His112, and a water molecule, and a distorted trigonal bipyramidal environment, which additionally comprises Glu73. Manual docking of the substrate quercetin into the active site showed that the different geometries of the copper site might be of catalytic importance	726503
1.13.11.24	homodimer	monocupin domain structure	-, 724015
1.13.11.24	monomer	1 * 55000, SDS-PAGE	685423

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Release 2023.1 (January 2023)