in complex with adenosine, inhibitors 2,2'-(2-(2-((2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-carboxamido)ethylamino)-2-oxoethylazanediyl) diacetic acid, baicalin and ADP analog AMPCP. The dimeric enzyme undergoes an extensive 114° conformational switch between the open and closed forms. The dimerization interface is formed by the C-terminal domains and exhibits interchain motions of up to 13°. Structural control of the domain movement determines the selectivity for monophosphate nucleotides |
Homo sapiens |