Dihydrodipicolinate synthase (DHDPS) from C.jejuni with pyruvate bound in the active site and L-histidine bound at the allosteric site
收藏Protein Data Bank Japan2023-11-29 更新2026-03-21 收录
下载链接：
https://pdbj.org/mine/summary/7kxg
下载链接
链接失效反馈官方服务：
资源简介：
Dihydrodipicolinate synthase (DHDPS) from C.jejuni with pyruvate bound in the active site and L-histidine bound at the allosteric site Descriptor: 1,2-ETHANEDIOL, 4-hydroxy-tetrahydrodipicolinate synthase, ACETATE ION, ... Authors: Saran, S, Sanders, D.A.R. Deposit date: 2020-12-03 Release date: 2021-12-08 Last modified: 2023-11-29 Method: X-RAY DIFFRACTION (2.28 Å) Cite: Reversing the roles of a crucial hydrogen-bonding pair: a lysine-insensitive mutant of Campylobacter jejuni dihydrodipicolinate synthase, H59K, binds histidine in its allosteric site To Be Published
源自空肠弯曲菌（Campylobacter jejuni, C.jejuni）的二氢二吡啶甲酸合酶（Dihydrodipicolinate synthase, DHDPS），其活性位点结合有丙酮酸，别构位点结合有L-组氨酸。
描述项：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.
提交日期：2020-12-03
发布日期：2021-12-08
最后修改日期：2023-11-29
实验方法：X射线衍射（分辨率2.28埃）
引用文献：《一对关键氢键对的角色反转：空肠弯曲菌二氢二吡啶甲酸合酶赖氨酸不敏感突变体H59K的别构位点结合组氨酸》，待发表
创建时间：
2020-12-03
