Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H56N mutant with pyruvate bound in the active site and L-lysine bound at the allosteric site
收藏Protein Data Bank Japan2023-11-29 更新2026-03-21 收录
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Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H56N mutant with pyruvate bound in the active site and L-lysine bound at the allosteric site Descriptor: 1,2-ETHANEDIOL, 4-hydroxy-tetrahydrodipicolinate synthase, ACETATE ION, ... Authors: Saran, S, Sanders, D.A.R. Deposit date: 2020-11-25 Release date: 2021-12-01 Last modified: 2023-11-29 Method: X-RAY DIFFRACTION (2.25 Å) Cite: ALLOSTERIC SITE RESIDUE 'H56' CAPS THE INHIBITOR AT THE TIGHT DIMER INTERFACE FOR TRANSMITTING THE ALLOSTERIC INHIBITION SIGNALS IN Cj.DHDPS To Be Published
来自空肠弯曲杆菌(C. jejuni)的二氢二吡啶甲酸合酶(Dihydrodipicolinate synthase, DHDPS)H56N突变体,其活性位点结合丙酮酸,别构位点(allosteric site)结合L-赖氨酸。描述符:1,2-乙二醇、4-羟基四氢二吡啶甲酸合酶、乙酸根离子……作者:Saran, S.、Sanders, D.A.R.。存档日期:2020-11-25;发布日期:2021-12-01;最后修改日期:2023-11-29。实验方法:X射线衍射(X-RAY DIFFRACTION,分辨率2.25 Å)。引用文献:《别构位点残基H56在Cj.DHDPS的紧密二聚体界面处封阻抑制剂以传递别构抑制信号》(待发表)
创建时间:
2020-11-25



