3EAI
| Structure of inhibited murine iNOS oxygenase domain | 分子名称: | 4-({4-[(4-methoxypyridin-2-yl)amino]piperidin-1-yl}carbonyl)benzonitrile, 5,6,7,8-TETRAHYDROBIOPTERIN, Nitric oxide synthase, ... | 著者 | Garcin, E.D, Arvai, A.S, Rosenfeld, R.J, Kroeger, M.D, Crane, B.R, Andersson, G, Andrews, G, Hamley, P.J, Mallinder, P.R, Nicholls, D.J, St-Gallay, S.A, Tinker, A.C, Gensmantel, N.P, Mete, A, Cheshire, D.R, Connolly, S, Stuehr, D.J, Aberg, A, Wallace, A.V, Tainer, J.A, Getzoff, E.D. | 登録日 | 2008-08-25 | 公開日 | 2008-10-07 | 最終更新日 | 2024-02-21 | 実験手法 | X-RAY DIFFRACTION (2.2 Å) | 主引用文献 | Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase. Nat.Chem.Biol., 4, 2008
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1DGB
| HUMAN ERYTHROCYTE CATALASE | 分子名称: | CATALASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, PROTOPORPHYRIN IX CONTAINING FE | 著者 | Putnam, C.D, Arvai, A.S, Bourne, Y, Tainer, J.A. | 登録日 | 1999-11-23 | 公開日 | 2000-02-11 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (2.2 Å) | 主引用文献 | Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J.Mol.Biol., 296, 2000
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1DGG
| HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX | 分子名称: | CATALASE, CYANIDE ION, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... | 著者 | Putnam, C.D, Arvai, A.S, Bourne, Y, Tainer, J.A. | 登録日 | 1999-11-24 | 公開日 | 2000-02-17 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J.Mol.Biol., 296, 2000
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1DGH
| HUMAN ERYTHROCYTE CATALASE 3-AMINO-1,2,4-TRIAZOLE COMPLEX | 分子名称: | NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, PROTEIN (CATALASE), PROTOPORPHYRIN IX CONTAINING FE | 著者 | Putnam, C.D, Arvai, A.S, Bourne, Y, Tainer, J.A. | 登録日 | 1999-11-24 | 公開日 | 2000-02-17 | 最終更新日 | 2023-08-09 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J.Mol.Biol., 296, 2000
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1DGF
| HUMAN ERYTHROCYTE CATALASE | 分子名称: | ACETATE ION, CATALASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... | 著者 | Putnam, C.D, Arvai, A.S, Bourne, Y, Tainer, J.A. | 登録日 | 1999-11-24 | 公開日 | 2000-02-11 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (1.5 Å) | 主引用文献 | Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J.Mol.Biol., 296, 2000
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4NCK
| Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation | 分子名称: | CHLORIDE ION, DNA double-strand break repair Rad50 ATPase, MAGNESIUM ION, ... | 著者 | Classen, S, Williams, G.J, Arvai, A.S, Williams, R.S. | 登録日 | 2013-10-24 | 公開日 | 2014-03-05 | 最終更新日 | 2024-02-28 | 実験手法 | X-RAY DIFFRACTION (1.99 Å) | 主引用文献 | ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling. Embo J., 33, 2014
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4NCI
| Crystal Structure of Pyrococcus furiosis Rad50 R805E mutation | 分子名称: | DNA double-strand break repair Rad50 ATPase | 著者 | Classen, S, Williams, G.J, Arvai, A.S, Williams, R.S. | 登録日 | 2013-10-24 | 公開日 | 2014-03-05 | 最終更新日 | 2024-02-28 | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | 主引用文献 | ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling. Embo J., 33, 2014
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4NCH
| Crystal Structure of Pyrococcus furiosis Rad50 L802W mutation | 分子名称: | DNA double-strand break repair Rad50 ATPase, SULFATE ION | 著者 | Classen, S, Williams, G.J, Arvai, A.S, Williams, R.S. | 登録日 | 2013-10-24 | 公開日 | 2014-03-05 | 最終更新日 | 2024-02-28 | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | 主引用文献 | ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling. Embo J., 33, 2014
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4NCJ
| Crystal Structure of Pyrococcus furiosis Rad50 R805E mutation with ADP Beryllium Flouride | 分子名称: | ADENOSINE-5'-DIPHOSPHATE, BERYLLIUM TRIFLUORIDE ION, DNA double-strand break repair Rad50 ATPase, ... | 著者 | Classen, S, Williams, G.J, Arvai, A.S, Williams, R.S. | 登録日 | 2013-10-24 | 公開日 | 2014-03-05 | 最終更新日 | 2024-02-28 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling. Embo J., 33, 2014
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