PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31854421-3 2020 Here by analogizing structurally related kinases and molecular dynamics simulations, we constructed a model of the MDD-substrate-ATP-Mg2+ complex and proposed that MDD requires two Mg2+ ions for maintaining a catalytically active conformation. Magnesium 133-137 mevalonate diphosphate decarboxylase Homo sapiens 115-118 31854421-3 2020 Here by analogizing structurally related kinases and molecular dynamics simulations, we constructed a model of the MDD-substrate-ATP-Mg2+ complex and proposed that MDD requires two Mg2+ ions for maintaining a catalytically active conformation. Magnesium 133-137 mevalonate diphosphate decarboxylase Homo sapiens 164-167 31854421-3 2020 Here by analogizing structurally related kinases and molecular dynamics simulations, we constructed a model of the MDD-substrate-ATP-Mg2+ complex and proposed that MDD requires two Mg2+ ions for maintaining a catalytically active conformation. Magnesium 181-185 mevalonate diphosphate decarboxylase Homo sapiens 115-118 31854421-3 2020 Here by analogizing structurally related kinases and molecular dynamics simulations, we constructed a model of the MDD-substrate-ATP-Mg2+ complex and proposed that MDD requires two Mg2+ ions for maintaining a catalytically active conformation. Magnesium 181-185 mevalonate diphosphate decarboxylase Homo sapiens 164-167