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Structure of the m17 leucyl aminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor

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Protein Data Bank Japan2023-09-20 更新2026-03-21 收录
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Structure of the m17 leucyl aminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor Descriptor: CARBONATE ION, DIMETHYL SULFOXIDE, M17 leucyl aminopeptidase, ... Authors: Drinkwater, N, Mcgowan, S. Deposit date: 2014-08-26 Release date: 2014-10-29 Last modified: 2023-09-20 Method: X-RAY DIFFRACTION (2.6 Å) Cite: Two-Pronged Attack: Dual Inhibition of Plasmodium falciparum M1 and M17 Metalloaminopeptidases by a Novel Series of Hydroxamic Acid-Based Inhibitors. J.Med.Chem., 57, 2014

疟原虫来源的M17亮氨酸氨肽酶(M17 leucyl aminopeptidase)与羟肟酸类抑制剂(hydroxamic acid-based inhibitor)结合的晶体结构 描述项:碳酸根离子(CARBONATE ION)、二甲基亚砜(DIMETHYL SULFOXIDE)、M17亮氨酸氨肽酶(M17 leucyl aminopeptidase)等 作者:N·德林克沃特(Drinkwater, N)、S·麦高恩(McGowan, S) 存档日期:2014-08-26 发布日期:2014-10-29 最后修改日期:2023-09-20 实验方法:X射线衍射(X-RAY DIFFRACTION),分辨率2.6埃(2.6 Å) 引用文献:《双重攻击:新型羟肟酸类抑制剂双重抑制恶性疟原虫M1及M17金属氨肽酶》,《药物化学杂志》(J.Med.Chem.),57卷,2014年
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2014-08-26
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