1CH4
| MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA (F133V) | 分子名称: | CARBON MONOXIDE, MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA, PROTOPORPHYRIN IX CONTAINING FE | 著者 | Shirai, T, Fujikake, M, Yamane, T, Inaba, K, Ishimori, K, Morishima, I. | 登録日 | 1998-06-11 | 公開日 | 1999-04-27 | 最終更新日 | 2024-04-03 | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | 主引用文献 | Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin beta alpha, at 2.5 A resolution. J.Mol.Biol., 287, 1999
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5ZR0
| Solution structure of peptidyl-prolyl cis/trans isomerase domain of Trigger Factor in complex with MBP | 分子名称: | Maltose-binding periplasmic protein,Trigger factor | 著者 | Kawagoe, S, Nakagawa, H, Kumeta, H, Ishimori, K, Saio, T. | 登録日 | 2018-04-21 | 公開日 | 2018-08-22 | 最終更新日 | 2024-05-01 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural insight into prolinecis/transisomerization of unfolded proteins catalyzed by the trigger factor chaperone. J. Biol. Chem., 293, 2018
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5H6O
| Porphobilinogen deaminase from Vibrio Cholerae | 分子名称: | 3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid, MAGNESIUM ION, Porphobilinogen deaminase | 著者 | Funamizu, T, Chen, M, Tanaka, Y, Ishimori, K, Uchida, T. | 登録日 | 2016-11-14 | 公開日 | 2017-11-15 | 最終更新日 | 2023-11-08 | 実験手法 | X-RAY DIFFRACTION (2.702 Å) | 主引用文献 | Porphobilinogen deaminase from Vibrio Cholerae To Be Published
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6D6S
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1T85
| Crystal Structure of the Ferrous CO-bound Cytochrome P450cam Mutant (L358P/C334A) | 分子名称: | CAMPHOR, CARBON MONOXIDE, Cytochrome P450-cam, ... | 著者 | Nagano, S, Tosha, T, Ishimori, K, Morishima, I, Poulos, T.L. | 登録日 | 2004-05-11 | 公開日 | 2004-06-01 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding. J.Biol.Chem., 279, 2004
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1T86
| Crystal Structure of the Ferrous Cytochrome P450cam Mutant (L358P/C334A) | 分子名称: | CAMPHOR, Cytochrome P450-cam, POTASSIUM ION, ... | 著者 | Nagano, S, Tosha, T, Ishimori, K, Morishima, I, Poulos, T.L. | 登録日 | 2004-05-11 | 公開日 | 2004-05-25 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding. J.Biol.Chem., 279, 2004
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1T87
| Crystal Structure of the Ferrous CO-bound Cytochrome P450cam (C334A) | 分子名称: | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, CAMPHOR, CARBON MONOXIDE, ... | 著者 | Nagano, S, Tosha, T, Ishimori, K, Morishima, I, Poulos, T.L. | 登録日 | 2004-05-11 | 公開日 | 2004-05-25 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding. J.Biol.Chem., 279, 2004
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1T88
| Crystal Structure of the Ferrous Cytochrome P450cam (C334A) | 分子名称: | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, CAMPHOR, Cytochrome P450-cam, ... | 著者 | Nagano, S, Tosha, T, Ishimori, K, Morishima, I, Poulos, T.L. | 登録日 | 2004-05-11 | 公開日 | 2004-05-25 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding. J.Biol.Chem., 279, 2004
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2N9J
| Solution structure of oxidized human cytochrome c | 分子名称: | Cytochrome c, HEME C | 著者 | Imai, M, Saio, T, Kumeta, H, Uchida, T, Inagaki, F, Ishimori, K. | 登録日 | 2015-11-24 | 公開日 | 2016-02-17 | 最終更新日 | 2023-06-14 | 実験手法 | SOLUTION NMR | 主引用文献 | Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c. Biochem.Biophys.Res.Commun., 469, 2016
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2N9I
| Solution structure of reduced human cytochrome c | 分子名称: | Cytochrome c, HEME C | 著者 | Imai, M, Saio, T, Kumeta, H, Uchida, T, Inagaki, F, Ishimori, K. | 登録日 | 2015-11-24 | 公開日 | 2016-02-17 | 最終更新日 | 2023-06-14 | 実験手法 | SOLUTION NMR | 主引用文献 | Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c Biochem.Biophys.Res.Commun., 469, 2016
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