1PHS
THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION
1PHS の概要
| エントリーDOI | 10.2210/pdb1phs/pdb |
| 分子名称 | PHASEOLIN, BETA-TYPE PRECURSOR (1 entity in total) |
| 機能のキーワード | plant seed storage protein (vicilin) |
| 由来する生物種 | Phaseolus vulgaris |
| 細胞内の位置 | Vacuole, aleurone grain: P02853 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 45043.04 |
| 構造登録者 | Lawrence, M.C.,Suzuki, E.,Varghese, J.N.,Davis, P.C.,Vandonkelaar, A.,Tulloch, P.A.,Colman, P.M. (登録日: 1990-03-21, 公開日: 1990-10-15, 最終更新日: 2023-09-27) |
| 主引用文献 | Lawrence, M.C.,Suzuki, E.,Varghese, J.N.,Davis, P.C.,Van Donkelaar, A.,Tulloch, P.A.,Colman, P.M. The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution. EMBO J., 9:9-15, 1990 Cited by PubMed Abstract: The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins. PubMed: 2295315主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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