Structural Models of Mammalian MsrBs
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下载链接：
https://figshare.com/articles/dataset/Different_Catalytic_Mechanisms_in_Mammalian_Selenocysteine_and_Cysteine_Containing_Methionine_R_Sulfoxide_Reductases/153536
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资源简介：
(A) Surface models of mouse MsrB2 and human MsrB3. Catalytic Cys95 residues are shown in red. Asn97 residues that sit at the bottom of the active-site pockets inMsrB2 and MsrB3 are shown in blue.
(B) Mouse MsrB1. In the structural model, the distance between Cys4 and Sec95 was ∼10 Å. A hinge consisting of Gly8 and Gly9 is shown in blue and indicated by arrows. Four Cys residues that coordinate Zn are shown in orange (the zinc atom is not shown).
(1.3 MB PDF).
(A) 小鼠MsrB2与人类MsrB3的表面结构模型。催化活性半胱氨酸（Cys）95残基以红色标注。位于MsrB2与MsrB3活性位点口袋底部的天冬酰胺（Asn）97残基以蓝色标注。
(B) 小鼠MsrB1的结构模型。该结构模型中，半胱氨酸（Cys）4与硒代半胱氨酸（Sec）95之间的距离约为10 Å。由甘氨酸（Gly）8与甘氨酸（Gly）9构成的铰链区域以蓝色标注，并以箭头标示。四个参与锌（Zn）配位的半胱氨酸（Cys）残基以橙色标注（未展示锌原子）。
(1.3 MB PDF)
创建时间：
2013-01-20
