2B5Z
Hen lysozyme chemically glycosylated
2B5Z の概要
| エントリーDOI | 10.2210/pdb2b5z/pdb |
| 関連するPDBエントリー | 132L 1IEE |
| 分子名称 | Lysozyme C, (1S)-1,5-anhydro-1-(ethylsulfonyl)-D-glucitol, AZIDE ION, ... (5 entities in total) |
| 機能のキーワード | chemical glycosylation, hydrolase |
| 由来する生物種 | Gallus gallus (chicken) |
| 細胞内の位置 | Secreted: P00698 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15574.41 |
| 構造登録者 | Lopez-Jaramillo, F.J.,Perez-Balderas, F.,Hernandez-Mateo, F.,Santoyo-Gonzalez, F. (登録日: 2005-09-29, 公開日: 2006-10-03, 最終更新日: 2024-10-30) |
| 主引用文献 | Lopez-Jaramillo, F.J.,Perez-Banderas, F.,Hernandez-Mateo, F.,Santoyo-Gonzalez, F. Production, crystallization and X-ray characterization of chemically glycosylated hen egg-white lysozyme. Acta Crystallogr.,Sect.F, 61:435-438, 2005 Cited by PubMed Abstract: The crystallization of glycoproteins is one of the challenges to be confronted by the crystallographic community in the frame of what is known as glycobiology. The state of the art for the crystallization of glycoproteins is not promising and removal of the carbohydrate chains is generally suggested since they are flexible and a source of heterogeneity. In this paper, the feasibility of introducing glucose into the model protein hen egg-white lysozyme via a post-purification glycosylation reaction that may turn any protein into a model glycoprotein whose carbohydrate fraction can be manipulated is demonstrated. PubMed: 16511062DOI: 10.1107/S1744309105008869 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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