Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum with mutated active site (R109A/K138A) and N-carbamoyl-L-phosphate bound

Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum with mutated active site (R109A/K138A) and N-carbamoyl-L-phosphate bound Descriptor: Aspartate transcarbamoylase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER Authors: Bosch, S.S, Lunev, S, Wrenger, C, Groves, M.R. Deposit date: 2018-09-10 Release date: 2018-09-26 Last modified: 2024-01-24 Method: X-RAY DIFFRACTION (2.5 Å) Cite: Molecular Target Validation of Aspartate Transcarbamoylase fromPlasmodium falciparumby Torin 2. Acs Infect Dis., 6, 2020

恶性疟原虫（Plasmodium falciparum）截短型天冬氨酸转氨甲酰酶（Aspartate transcarbamoylase），其活性位点发生R109A/K138A突变且结合N-氨基甲酰-L-磷酸（N-carbamoyl-L-phosphate）的晶体结构。描述符：天冬氨酸转氨甲酰酶（Aspartate transcarbamoylase）、磷酸单(甲酰胺)酯（PHOSPHORIC ACID MONO(FORMAMIDE)ESTER）。作者：Bosch, S.S.、Lunev, S.、Wrenger, C.、Groves, M.R.。提交日期：2018-09-10；发布日期：2018-09-26；最后修改日期：2024-01-24。实验方法：X射线衍射（X-RAY DIFFRACTION），分辨率2.5埃。引用：《通过Torin 2验证恶性疟原虫天冬氨酸转氨甲酰酶的分子靶点》，发表于《ACS感染性疾病》，第6卷，2020年。