3AQ9
| Crystal structure of truncated hemoglobin from Tetrahymena pyriformis, Q50E mutant, Fe(III) form | 分子名称: | Group 1 truncated hemoglobin, PROTOPORPHYRIN IX CONTAINING FE | 著者 | Igarashi, J, Kobayashi, K, Matsuoka, A. | 登録日 | 2010-10-25 | 公開日 | 2011-04-20 | 最終更新日 | 2023-11-01 | 実験手法 | X-RAY DIFFRACTION (1.74 Å) | 主引用文献 | A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification. J.Biol.Inorg.Chem., 16, 2011
|
|
3AQ8
| Crystal structure of truncated hemoglobin from Tetrahymena pyriformis, Q46E mutant, Fe(III) form | 分子名称: | Group 1 truncated hemoglobin, PROTOPORPHYRIN IX CONTAINING FE | 著者 | Igarashi, J, Kobayashi, K, Matsuoka, A. | 登録日 | 2010-10-25 | 公開日 | 2011-04-20 | 最終更新日 | 2023-11-01 | 実験手法 | X-RAY DIFFRACTION (1.83 Å) | 主引用文献 | A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification. J.Biol.Inorg.Chem., 16, 2011
|
|
3AQ6
| |
3AQ7
| Crystal structure of truncated hemoglobin from Tetrahymena pyriformis, Y25F mutant, Fe(III) form | 分子名称: | Group 1 truncated hemoglobin, PROTOPORPHYRIN IX CONTAINING FE | 著者 | Igarashi, J, Kobayashi, K, Matsuoka, A. | 登録日 | 2010-10-25 | 公開日 | 2011-04-20 | 最終更新日 | 2023-11-01 | 実験手法 | X-RAY DIFFRACTION (1.77 Å) | 主引用文献 | A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification. J.Biol.Inorg.Chem., 16, 2011
|
|
3AQ5
| Crystal structure of truncated hemoglobin from Tetrahymena pyriformis, Fe(II)-O2 form | 分子名称: | Group 1 truncated hemoglobin, OXYGEN MOLECULE, PROTOPORPHYRIN IX CONTAINING FE | 著者 | Igarashi, J, Kobayashi, K, Matsuoka, A. | 登録日 | 2010-10-25 | 公開日 | 2011-04-20 | 最終更新日 | 2023-11-01 | 実験手法 | X-RAY DIFFRACTION (1.78 Å) | 主引用文献 | A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification. J.Biol.Inorg.Chem., 16, 2011
|
|