A non-biological ATP binding protein with a single point mutation (D65V), that contributes to optimized folding and ligand binding, crystallized in the presence of 100 mM ATP.

A non-biological ATP binding protein with a single point mutation (D65V), that contributes to optimized folding and ligand binding, crystallized in the presence of 100 mM ATP. Descriptor: ADENOSINE-5'-DIPHOSPHATE, ATP BINDING PROTEIN-D65V, CHLORIDE ION, ... Authors: Simmons, C.R, Magee, C.L, Allen, J.P, Chaput, J.C. Deposit date: 2010-02-15 Release date: 2010-09-22 Last modified: 2023-09-06 Method: X-RAY DIFFRACTION (2.55 Å) Cite: Three-dimensional structures reveal multiple ADP/ATP binding modes for a synthetic class of artificial proteins. Biochemistry, 49, 2010

一种携带单点突变D65V的非生物源三磷酸腺苷（ATP）结合蛋白，该突变可优化蛋白折叠与配体结合特性，此蛋白在100 mM ATP存在的条件下完成结晶。描述符：腺苷-5'-二磷酸（ADENOSINE-5'-DIPHOSPHATE）、ATP结合蛋白-D65V、氯离子（CHLORIDE ION）……作者：西蒙斯（Simmons, C.R）、梅奇（Magee, C.L）、艾伦（Allen, J.P）、查普特（Chaput, J.C）。提交日期：2010-02-15；发布日期：2010-09-22；最后修改日期：2023-09-06。实验方法：X射线衍射（X-RAY DIFFRACTION，分辨率2.55埃（Å））。引用文献：《三维结构揭示一类人工合成蛋白的多种ADP/ATP结合模式》，《生物化学（Biochemistry）》，第49卷，2010年