1QIV
 
 | | CALMODULIN COMPLEXED WITH N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-(3,4-BIS-BUTOXYPHENYL)-ETHYL]-PROPYLENEDIAMINE (DPD), 1:2 COMPLEX | | 分子名称: | CALCIUM ION, CALMODULIN, N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-(2 3,4-BIS-BUTOXYPHENYL)-ETHYL]-PROPYLENEDIAMINE | | 著者 | Harmat, V, Bocskei, Z.S, Vertessy, B.G, Naray-Szabo, G, Ovadi, J. | | 登録日 | 1999-06-17 | | 公開日 | 2000-03-28 | | 最終更新日 | 2023-12-13 | | 実験手法 | X-RAY DIFFRACTION (2.64 Å) | | 主引用文献 | A New Potent Calmodulin Antagonist with Arylalkylamine Structure: Crystallographic, Spectroscopic and Functional Studies
J.Mol.Biol., 297, 2000
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1QIW
 | | Calmodulin complexed with N-(3,3,-diphenylpropyl)-N'-[1-R-(3,4-bis-butoxyphenyl)-ethyl]-propylenediamine (DPD) | | 分子名称: | CALCIUM ION, CALMODULIN, N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-(2 3,4-BIS-BUTOXYPHENYL)-ETHYL]-PROPYLENEDIAMINE | | 著者 | Harmat, V, Bocskei, Z.S, Vertessy, B.G, Ovadi, J, Naray-Szabo, G. | | 登録日 | 1999-06-17 | | 公開日 | 2000-03-28 | | 最終更新日 | 2023-12-13 | | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | | 主引用文献 | A New Potent Calmodulin Antagonist with Arylalkylamine Structure: Crystallographic, Spectroscopic and Functional Studies
J.Mol.Biol., 297, 2000
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1XLM
 | | D254E, D256E MUTANT OF D-XYLOSE ISOMERASE COMPLEXED WITH AL3 AND XYLITOL | | 分子名称: | ALUMINUM ION, D-XYLOSE ISOMERASE, Xylitol | | 著者 | Gerczei, T, Bocskei, Z.S, Szabo, E, Naray-Szabo, G, Asboth, B. | | 登録日 | 1997-07-22 | | 公開日 | 1998-01-28 | | 最終更新日 | 2024-05-22 | | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | | 主引用文献 | Structure determination and refinement of the Al3+ complex of the D254,256E mutant of Arthrobacter D-xylose isomerase at 2.40 A resolution. Further evidence for inhibitor-induced metal ion movement.
Int.J.Biol.Macromol., 25, 1999
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1AMH
 | | UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S) | | 分子名称: | ANIONIC TRYPSIN, CALCIUM ION | | 著者 | Szabo, E, Bocskei, Z.S, Naray-Szabo, G, Graf, L. | | 登録日 | 1997-06-17 | | 公開日 | 1997-12-24 | | 最終更新日 | 2023-08-02 | | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | | 主引用文献 | The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the protease.
Eur.J.Biochem., 263, 1999
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