5DK8
Human ubiquitin in the P1 space group
5DK8 の概要
| エントリーDOI | 10.2210/pdb5dk8/pdb |
| 分子名称 | Polyubiquitin-B, MAGNESIUM ION (3 entities in total) |
| 機能のキーワード | signaling protein |
| 由来する生物種 | Homo sapiens (Human) |
| 細胞内の位置 | Ubiquitin: Cytoplasm : P0CG47 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 17354.06 |
| 構造登録者 | |
| 主引用文献 | Camara-Artigas, A.,Plaza-Garrido, M.,Martinez-Rodriguez, S.,Bacarizo, J. New crystal form of human ubiquitin in the presence of magnesium. Acta Crystallogr.,Sect.F, 72:29-35, 2016 Cited by PubMed Abstract: Ubiquitin is a small globular protein that has a considerable number of lysine residues on its surface. This results in a high surface entropy that precludes the formation of crystal-packing interactions. To date, only a few structures of the native form of ubiquitin have been solved, and most of the crystals that led to these structures were obtained in the presence of different divalent metal cations. In this work, a new crystallographic structure of human ubiquitin solved from crystals grown in the presence of magnesium is presented. The crystals belonged to a triclinic space group, with unit-cell parameters a = 29.96, b = 30.18, c = 41.41 Å, α = 88.52, β = 79.12, γ = 67.37°. The crystal lattice is composed of stacked layers of human ubiquitin molecules with a large hydrophobic interface and a smaller polar interface in which the magnesium ion lies at the junction between adjacent layers in the crystal. The metal ion appears in a hexa-aquo coordination, which is key to facilitating the crystallization of the protein. PubMed: 26750481DOI: 10.1107/S2053230X15023390 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.32 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






