Crystal structure of the iGluR2 ligand-binding core (S1S2J-N754S) in complex with glutamate and NS5206 at 2.10 A resolution
收藏Protein Data Bank Japan2024-10-16 更新2026-03-21 收录
下载链接:
https://pdbj.org/mine/summary/3h6v
下载链接
链接失效反馈官方服务:
资源简介:
Crystal structure of the iGluR2 ligand-binding core (S1S2J-N754S) in complex with glutamate and NS5206 at 2.10 A resolution Descriptor: (3R)-3-cyclopentyl-7-[(4-methylpiperazin-1-yl)sulfonyl]-3,4-dihydro-2H-1,2-benzothiazine 1,1-dioxide, DIMETHYL SULFOXIDE, GLUTAMIC ACID, ... Authors: Hald, H, Gajhede, M, Kastrup, J.S. Deposit date: 2009-04-24 Release date: 2009-07-28 Last modified: 2024-10-16 Method: X-RAY DIFFRACTION (2.1 Å) Cite: Distinct structural features of cyclothiazide are responsible for effects on peak current amplitude and desensitization kinetics at iGluR2. J.Mol.Biol., 391, 2009
分辨率2.10埃的iGluR2配体结合核心结构域(S1S2J-N754S)与谷氨酸及NS5206形成复合物的晶体结构。描述符:(3R)-3-环戊基-7-[(4-甲基哌嗪-1-基)磺酰基]-3,4-二氢-2H-1,2-苯并噻嗪-1,1-二氧化物、二甲基亚砜(DIMETHYL SULFOXIDE)、谷氨酸(GLUTAMIC ACID)等。作者:Hald H、Gajhede M、Kastrup J.S.。提交日期:2009年4月24日,发布日期:2009年7月28日,最后修改日期:2024年10月16日。实验方法:X射线衍射(X-RAY DIFFRACTION)(分辨率2.1埃)。引用文献:《环噻嗪的独特结构特征决定其对iGluR2的峰值电流幅度与脱敏动力学的影响》,J.Mol.Biol., 391, 2009。
创建时间:
2009-04-24



