2XJH
| Structure and Copper-binding Properties of Methanobactins from Methylosinus trichosporium OB3b | 分子名称: | COPPER (II) ION, METHANOBACTIN MB-OB3B, SODIUM ION | 著者 | El-Ghazouani, A, Basle, A, Firbank, S.J, Knapp, C.W, Gray, J, Graham, D.W, Dennison, C. | 登録日 | 2010-07-06 | 公開日 | 2011-02-02 | 最終更新日 | 2024-10-23 | 実験手法 | X-RAY DIFFRACTION (0.92 Å) | 主引用文献 | Copper-Binding Properties and Structures of Methanobactins from Methylosinus Trichosporium Ob3B. Inorg.Chem., 50, 2011
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2XJI
| Structure and Copper-binding Properties of Methanobactins from Methylosinus trichosporium OB3b | 分子名称: | COPPER (II) ION, METHANOBACTIN MB-OB3B | 著者 | El-Ghazouani, A, Basle, A, Firbank, S.J, Knapp, C.W, Gray, J, Graham, D.W, Dennison, C. | 登録日 | 2010-07-06 | 公開日 | 2011-02-02 | 最終更新日 | 2024-11-06 | 実験手法 | X-RAY DIFFRACTION (1 Å) | 主引用文献 | Copper-Binding Properties and Structures of Methanobactins from Methylosinus Trichosporium Ob3B. Inorg.Chem., 50, 2011
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4OZ7
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2YGI
| Methanobactin HM1 | 分子名称: | COPPER (II) ION, METHANOBACTIN HM1 | 著者 | Ghazouani, A, Basle, A, Firbank, S.J, Gray, J, Dennison, C. | 登録日 | 2011-04-18 | 公開日 | 2012-04-25 | 最終更新日 | 2023-11-15 | 実験手法 | X-RAY DIFFRACTION (0.8 Å) | 主引用文献 | Variations in Methanobactin Structure Influences Copper Utilization by Methane-Oxidizing Bacteria. Proc.Natl.Acad.Sci.USA, 109, 2012
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2YGJ
| Methanobactin MB4 | 分子名称: | COPPER (II) ION, METHANOBACTIN MB4, SODIUM ION | 著者 | Ghazouani, A, Basle, A, Firbank, S.J, Gray, J, Dennison, C. | 登録日 | 2011-04-18 | 公開日 | 2012-04-25 | 最終更新日 | 2023-11-15 | 実験手法 | X-RAY DIFFRACTION (0.8 Å) | 主引用文献 | Variations in Methanobactin Structure Influences Copper Utilization by Methane-Oxidizing Bacteria. Proc.Natl.Acad.Sci.USA, 109, 2012
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2FE3
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2RGV
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3F8N
| Crystal structure of PerR-Zn-Mn | 分子名称: | MANGANESE (II) ION, Peroxide operon regulator, ZINC ION | 著者 | Traore, D.A.K, Ferrer, J.-L, Jacquamet, L, Duarte, V, Latour, J.-M. | 登録日 | 2008-11-13 | 公開日 | 2009-06-16 | 最終更新日 | 2023-11-01 | 実験手法 | X-RAY DIFFRACTION (3.15 Å) | 主引用文献 | Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding Mol.Microbiol., 73, 2009
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