4GYL
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![BU of 4gyl by Molmil](/molmil-images/mine/4gyl) | The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine | 分子名称: | Aliphatic amidase, CHLORIDE ION, PROPIONAMIDE | 著者 | Weber, B.W, Sewell, B.T, Kimani, S.W, Varsani, A, Cowan, D.A, Hunter, R. | 登録日 | 2012-09-05 | 公開日 | 2013-08-21 | 最終更新日 | 2014-02-05 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J.Biol.Chem., 288, 2013
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4GYN
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![BU of 4gyn by Molmil](/molmil-images/mine/4gyn) | The E142L mutant of the amidase from Geobacillus pallidus | 分子名称: | Aliphatic amidase, CHLORIDE ION | 著者 | Weber, B.W, Sewell, B.T, Kimani, S.W, Varsani, A, Cowan, D.A, Hunter, R. | 登録日 | 2012-09-05 | 公開日 | 2013-08-21 | 最終更新日 | 2023-11-08 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J.Biol.Chem., 288, 2013
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4KZF
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![BU of 4kzf by Molmil](/molmil-images/mine/4kzf) | The mechanism of the amidases: The effect of the mutation E142L in the amidase from Geobacillus pallidus | 分子名称: | Aliphatic amidase, CHLORIDE ION | 著者 | Weber, B.W, Sewell, B.T, Kimani, S.W, Varsani, A, Cowan, D.A, Hunter, R. | 登録日 | 2013-05-29 | 公開日 | 2013-08-21 | 最終更新日 | 2023-11-08 | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | 主引用文献 | The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J.Biol.Chem., 288, 2013
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4LF0
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![BU of 4lf0 by Molmil](/molmil-images/mine/4lf0) | The E142D mutant of the amidase from Geobacillus pallidus | 分子名称: | Aliphatic amidase | 著者 | Sewell, B.T, Weber, B.W, Kimani, S.W, Cowan, D.A, Hunter, R, Venter, G.A, Gumbart, J.C, Thuku, R.N, Varsani, A. | 登録日 | 2013-06-26 | 公開日 | 2013-08-21 | 最終更新日 | 2024-03-20 | 実験手法 | X-RAY DIFFRACTION (1.1 Å) | 主引用文献 | The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J.Biol.Chem., 288, 2013
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