5C4K
APH(2")-IVa in complex with GET (G418) at room temperature
5C4K の概要
| エントリーDOI | 10.2210/pdb5c4k/pdb |
| 分子名称 | APH(2'')-Id, GENETICIN (2 entities in total) |
| 機能のキーワード | aminoglycoside phosphotransferase, antibiotic resistance, transferase |
| 由来する生物種 | Enterococcus casseliflavus |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 75688.26 |
| 構造登録者 | Kaplan, E.,Guichou, J.F.,Berrou, K.,Chaloin, L.,Leban, N.,Lallemand, P.,Barman, T.,Serpersu, E.H.,Lionne, C. (登録日: 2015-06-18, 公開日: 2016-02-03, 最終更新日: 2024-01-10) |
| 主引用文献 | Kaplan, E.,Guichou, J.F.,Chaloin, L.,Kunzelmann, S.,Leban, N.,Serpersu, E.H.,Lionne, C. Aminoglycoside binding and catalysis specificity of aminoglycoside 2-phosphotransferase IVa: A thermodynamic, structural and kinetic study. Biochim.Biophys.Acta, 1860:802-813, 2016 Cited by PubMed Abstract: Aminoglycoside O-phosphotransferases make up a large class of bacterial enzymes that is widely distributed among pathogens and confer a high resistance to several clinically used aminoglycoside antibiotics. Aminoglycoside 2″-phosphotransferase IVa, APH(2″)-IVa, is an important member of this class, but there is little information on the thermodynamics of aminoglycoside binding and on the nature of its rate-limiting step. PubMed: 26802312DOI: 10.1016/j.bbagen.2016.01.016 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.05 Å) |
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