1GC5
CRYSTAL STRUCTURE OF A NOVEL ADP-DEPENDENT GLUCOKINASE FROM THERMOCOCCUS LITORALIS
1GC5 の概要
| エントリーDOI | 10.2210/pdb1gc5/pdb |
| 分子名称 | ADP-DEPENDENT GLUCOKINASE, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| 機能のキーワード | alfa/beta sandwichs, induced-fitting, transferase |
| 由来する生物種 | Thermococcus litoralis |
| 細胞内の位置 | Cytoplasm (By similarity): Q7M537 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 54045.29 |
| 構造登録者 | Ito, S.,Fushinobu, S.,Yoshioka, I.,Koga, S.,Matsuzawa, H.,Wakagi, T. (登録日: 2000-07-20, 公開日: 2001-07-25, 最終更新日: 2023-12-27) |
| 主引用文献 | Ito, S.,Fushinobu, S.,Yoshioka, I.,Koga, S.,Matsuzawa, H.,Wakagi, T. Structural Basis for the ADP-Specificity of a Novel Glucokinase from a Hyperthermophilic Archaeon Structure, 9:205-214, 2001 Cited by PubMed Abstract: ATP is the most common phosphoryl group donor for kinases. However, certain hyperthermophilic archaea such as Thermococcus litoralis and Pyrococcus furiosus utilize unusual ADP-dependent glucokinases and phosphofructokinases in their glycolytic pathways. These ADP-dependent kinases are homologous to each other but show no sequence similarity to any of the hitherto known ATP-dependent enzymes. PubMed: 11286887DOI: 10.1016/S0969-2126(01)00577-9 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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