5LGZ
Structure of Photoreduced Pentaerythritol Tetranitrate Reductase
5LGZ の概要
| エントリーDOI | 10.2210/pdb5lgz/pdb |
| 分子名称 | Pentaerythritol tetranitrate reductase, ISOPROPYL ALCOHOL, 1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL, ... (4 entities in total) |
| 機能のキーワード | petnr, petn reductase, fmn, fnr, photoreduction, oxidoreductase |
| 由来する生物種 | Enterobacter cloacae |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 39895.47 |
| 構造登録者 | |
| 主引用文献 | Kwon, H.,Smith, O.,Raven, E.L.,Moody, P.C. Combining X-ray and neutron crystallography with spectroscopy. Acta Crystallogr D Struct Biol, 73:141-147, 2017 Cited by PubMed Abstract: X-ray protein crystallography has, through the determination of the three-dimensional structures of enzymes and their complexes, been essential to the understanding of biological chemistry. However, as X-rays are scattered by electrons, the technique has difficulty locating the presence and position of H atoms (and cannot locate H ions), knowledge of which is often crucially important for the understanding of enzyme mechanism. Furthermore, X-ray irradiation, through photoelectronic effects, will perturb the redox state in the crystal. By using single-crystal spectrophotometry, reactions taking place in the crystal can be monitored, either to trap intermediates or follow photoreduction during X-ray data collection. By using neutron crystallography, the positions of H atoms can be located, as it is the nuclei rather than the electrons that scatter neutrons, and the scattering length is not determined by the atomic number. Combining the two techniques allows much greater insight into both reaction mechanism and X-ray-induced photoreduction. PubMed: 28177310DOI: 10.1107/S2059798316016314 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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