1RPW
| Crystal Structure Of The Multidrug Binding Protein Qacr Bound To The Diamidine Hexamidine | 分子名称: | 4,4'[1,6-HEXANEDIYLBIS(OXY)]BISBENZENECARBOXIMIDAMIDE, SULFATE ION, Transcriptional regulator qacR | 著者 | Murray, D.S, Schumacher, M.A, Brennan, R.G. | 登録日 | 2003-12-03 | 公開日 | 2004-06-01 | 最終更新日 | 2023-08-23 | 実験手法 | X-RAY DIFFRACTION (2.9 Å) | 主引用文献 | Crystal structures of QacR-diamidine complexes reveal additional multidrug-binding modes and a novel mechanism of drug charge neutralization. J.Biol.Chem., 279, 2004
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1RKW
| CRYSTAL STRUCTURE OF THE MULTIDRUG BINDING TRANSCRIPTIONAL REPRESSOR QACR BOUND TO PENTAMADINE | 分子名称: | 1,5-BIS(4-AMIDINOPHENOXY)PENTANE, SULFATE ION, Transcriptional regulator qacR | 著者 | Murray, D.S, Schumacher, M.A, Brennan, R.G. | 登録日 | 2003-11-23 | 公開日 | 2004-06-01 | 最終更新日 | 2023-08-23 | 実験手法 | X-RAY DIFFRACTION (2.62 Å) | 主引用文献 | Crystal structures of QacR-diamidine complexes reveal additional multidrug-binding modes and a novel mechanism of drug charge neutralization. J.Biol.Chem., 279, 2004
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4LNN
| B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of apo form of GS | 分子名称: | Glutamine synthetase, MAGNESIUM ION, SULFATE ION | 著者 | Schumacher, M.A, Chinnam, N, Tonthat, N, Fisher, S, Wray, L. | 登録日 | 2013-07-11 | 公開日 | 2013-11-13 | 最終更新日 | 2023-09-20 | 実験手法 | X-RAY DIFFRACTION (3.1 Å) | 主引用文献 | Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism. J.Biol.Chem., 288, 2013
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4LNI
| B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex | 分子名称: | ADENOSINE-5'-DIPHOSPHATE, Glutamine synthetase, L-METHIONINE-S-SULFOXIMINE PHOSPHATE, ... | 著者 | Schumacher, M.A, Chinnam, N, Tonthat, N, Fisher, S, Wray, L. | 登録日 | 2013-07-11 | 公開日 | 2013-11-06 | 最終更新日 | 2024-02-28 | 実験手法 | X-RAY DIFFRACTION (2.5793 Å) | 主引用文献 | Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism. J.Biol.Chem., 288, 2013
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4LNO
| B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: form two of GS-1 | 分子名称: | GLUTAMINE, Glutamine synthetase, MAGNESIUM ION | 著者 | Schumacher, M.A, Chinnam, N, Tonthat, N, Fisher, S, Wray, L. | 登録日 | 2013-07-11 | 公開日 | 2013-11-13 | 最終更新日 | 2023-09-20 | 実験手法 | X-RAY DIFFRACTION (2.9 Å) | 主引用文献 | Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism. J.Biol.Chem., 288, 2013
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4LNK
| B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-glutamate-AMPPCP complex | 分子名称: | ADENOSINE-5'-DIPHOSPHATE, GLUTAMIC ACID, Glutamine synthetase, ... | 著者 | Schumacher, M.A, Chinnam, N, Tonthat, N, Fisher, S, Wray, L. | 登録日 | 2013-07-11 | 公開日 | 2013-10-30 | 最終更新日 | 2023-09-20 | 実験手法 | X-RAY DIFFRACTION (2.87 Å) | 主引用文献 | Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism. J.Biol.Chem., 288, 2013
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4LNF
| B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-Q | 分子名称: | GLUTAMINE, Glutamine synthetase, MAGNESIUM ION, ... | 著者 | Schumacher, M.A, Chinnam, N, Tonthat, N, Fisher, S, Wray, L. | 登録日 | 2013-07-11 | 公開日 | 2013-11-13 | 最終更新日 | 2023-09-20 | 実験手法 | X-RAY DIFFRACTION (2.949 Å) | 主引用文献 | Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism. J.Biol.Chem., 288, 2013
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