7KWD
Crystal structure of Thermus thermophilus alkaline phosphatase
7KWD の概要
| エントリーDOI | 10.2210/pdb7kwd/pdb |
| 分子名称 | Alkaline phosphatase, L(+)-TARTARIC ACID, MAGNESIUM ION, ... (5 entities in total) |
| 機能のキーワード | homodimeric enzyme, dephosphorylate compounds, hydrolase |
| 由来する生物種 | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 110322.57 |
| 構造登録者 | Gallo, G.,Coelho, C.,Borges, B.,Negri, N.,Maiello, F.,Hardy, L.,Wurtele, M. (登録日: 2020-11-30, 公開日: 2021-04-14, 最終更新日: 2023-10-18) |
| 主引用文献 | Borges, B.,Gallo, G.,Coelho, C.,Negri, N.,Maiello, F.,Hardy, L.,Wurtele, M. Dynamic cross correlation analysis of Thermus thermophilus alkaline phosphatase and determinants of thermostability. Biochim Biophys Acta Gen Subj, 1865:129895-129895, 2021 Cited by PubMed Abstract: Understanding the determinants of protein thermostability is very important both from the theoretical and applied perspective. One emerging view in thermostable enzymes seems to indicate that a salt bridge/charged residue network plays a fundamental role in their thermostability. PubMed: 33781823DOI: 10.1016/j.bbagen.2021.129895 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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