Crystal structure of copper-bound tyrosinase from Streptomyces castaneoglobisporus in complex with the caddie protein obtained by soaking in the hydroxylamine-containing solution for 1 h at 277 K
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Crystal structure of copper-bound tyrosinase from Streptomyces castaneoglobisporus in complex with the caddie protein obtained by soaking in the hydroxylamine-containing solution for 1 h at 277 K Descriptor: COPPER (II) ION, MelC, NITRATE ION, ... Authors: Matoba, Y, Sugiyama, M. Deposit date: 2017-12-19 Release date: 2018-12-26 Last modified: 2025-09-17 Method: X-RAY DIFFRACTION (1.32 Å) Cite: Catalytic mechanism of tyrosinase implied from the quinone formation on the Tyr98 residue of the caddie protein To Be Published
栗色球孢链霉菌（Streptomyces castaneoglobisporus）来源的铜结合酪氨酸酶与伴侣蛋白（caddie protein）复合物的晶体结构：该复合物通过在含羟胺的溶液中于277K条件下浸泡1小时获得。
描述符：铜(II)离子、MelC、硝酸根离子等。
作者：Matoba, Y.、Sugiyama, M.
提交日期：2017-12-19
发布日期：2018-12-26
最后修改日期：2025-09-17
实验方法：X射线衍射（X-RAY DIFFRACTION），分辨率1.32埃
引用文献：《酪氨酸酶伴侣蛋白Tyr98位点醌形成揭示的酪氨酸酶催化机制》（Catalytic mechanism of tyrosinase implied from the quinone formation on the Tyr98 residue of the caddie protein），待发表
创建时间：
2017-12-19
