6JBD
Phosphotransferase-ATP complex related to CoA biosynthesis pathway
6JBD の概要
| エントリーDOI | 10.2210/pdb6jbd/pdb |
| 分子名称 | Pantoate kinase, GLYCEROL, 1,2-ETHANEDIOL, ... (9 entities in total) |
| 機能のキーワード | coa biosynthesis, transferase |
| 由来する生物種 | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 33975.91 |
| 構造登録者 | Kita, A.,Kishimoto, A.,Shimosaka, T.,Tomita, H.,Yokooji, Y.,Imanaka, T.,Atomi, H.,Miki, K. (登録日: 2019-01-25, 公開日: 2020-01-29, 最終更新日: 2024-03-27) |
| 主引用文献 | Kita, A.,Kishimoto, A.,Shimosaka, T.,Tomita, H.,Yokooji, Y.,Imanaka, T.,Atomi, H.,Miki, K. Crystal structure of pantoate kinase from Thermococcus kodakarensis. Proteins, 88:718-724, 2020 Cited by PubMed Abstract: The coenzyme A biosynthesis pathways in most archaea involve two unique enzymes, pantoate kinase and phosphopantothenate synthetase, to convert pantoate to 4'-phosphopantothenate. Here, we report the first crystal structure of pantoate kinase from the hyperthermophilic archaeon, Thermococcus kodakarensis and its complex with ATP and a magnesium ion. The electron density for the adenosine moiety of ATP was very weak, which most likely relates to its broad nucleotide specificity. Based on the structure of the active site that contains a glycerol molecule, the pantoate binding site and the roles of the highly conserved residues are suggested. PubMed: 31697438DOI: 10.1002/prot.25852 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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