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Crystal structure of the mutant V155S of orotidine 5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum complexed with inhibitor BMP

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Protein Data Bank Japan2024-03-20 更新2026-03-21 收录
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Crystal structure of the mutant V155S of orotidine 5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum complexed with inhibitor BMP Descriptor: 6-HYDROXYURIDINE-5'-PHOSPHATE, GLYCEROL, Orotidine 5'-phosphate decarboxylase Authors: Fedorov, A.A, Fedorov, E.V, Wood, B.M, Gerlt, J.A, Almo, S.C. Deposit date: 2010-06-29 Release date: 2011-05-11 Last modified: 2024-03-20 Method: X-RAY DIFFRACTION (1.32 Å) Cite: Mechanism of the orotidine 5'-monophosphate decarboxylase-catalyzed reaction: importance of residues in the orotate binding site. Biochemistry, 50, 2011

嗜热自养甲烷杆菌(Methanobacterium thermoautotrophicum)来源的乳清苷-5'-单磷酸脱羧酶(orotidine 5'-monophosphate decarboxylase)V155S突变体与抑制剂BMP结合的晶体结构。描述项:6-羟基尿苷-5'-磷酸(6-HYDROXYURIDINE-5'-PHOSPHATE)、甘油(GLYCEROL)、乳清苷-5'-磷酸脱羧酶(Orotidine 5'-phosphate decarboxylase)。作者:Fedorov, A.A、Fedorov, E.V、Wood, B.M、Gerlt, J.A、Almo, S.C。提交日期:2010年6月29日;发布日期:2011年5月11日;最后修改日期:2024年3月20日。实验方法:X射线衍射(X-RAY DIFFRACTION),分辨率1.32埃。引用文献:《乳清苷-5'-单磷酸脱羧酶催化反应的机制:乳清酸结合位点残基的重要性》,《生物化学(Biochemistry)》,第50卷,2011年。
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2010-06-29
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