1R0M
 
 | | Structure of Deinococcus radiodurans N-acylamino acid racemase at 1.3 : insights into a flexible binding pocket and evolution of enzymatic activity | | 分子名称: | N-acylamino acid racemase | | 著者 | Wang, W.-C, Chiu, W.-C, Hsu, S.-K, Wu, C.-L, Chen, C.-Y, Liu, J.-S, Hsu, W.-H. | | 登録日 | 2003-09-22 | | 公開日 | 2004-09-22 | | 最終更新日 | 2024-03-13 | | 実験手法 | X-RAY DIFFRACTION (1.3 Å) | | 主引用文献 | Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans
J.Mol.Biol., 342, 2004
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1XS2
 | | Structural Basis for Catalytic Racemization and Substrate Specificity of an N-Acylamino Acid Racemase Homologue from Deinococcus radiodurans | | 分子名称: | MAGNESIUM ION, N-Acylamino Acid Racemase | | 著者 | Wang, W.-C, Chiu, W.-C, Hsu, S.-K, Wu, C.-L, Chen, C.-Y, Liu, J.-S, Hsu, W.-H. | | 登録日 | 2004-10-18 | | 公開日 | 2004-11-02 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | | 主引用文献 | Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans
J.Mol.Biol., 342, 2004
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1XPY
 | | Structural Basis for Catalytic Racemization and Substrate Specificity of an N-Acylamino Acid Racemase Homologue from Deinococcus radiodurans | | 分子名称: | MAGNESIUM ION, N-acylamino acid racemase, N~2~-ACETYL-L-GLUTAMINE | | 著者 | Wang, W.-C, Chiu, W.-C, Hsu, S.-K, Wu, C.-L, Chen, C.-Y, Liu, J.-S, Hsu, W.-H. | | 登録日 | 2004-10-10 | | 公開日 | 2004-10-26 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | | 主引用文献 | Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans
J.Mol.Biol., 342, 2004
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1FO6
 | | CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE | | 分子名称: | N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE, XENON | | 著者 | Wang, W.-C, Hsu, W.-H, Chien, F.-T, Chen, C.-Y. | | 登録日 | 2000-08-25 | | 公開日 | 2001-08-29 | | 最終更新日 | 2024-03-13 | | 実験手法 | X-RAY DIFFRACTION (1.95 Å) | | 主引用文献 | Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft.
J.Mol.Biol., 306, 2001
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