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3H5G

Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides.

3H5G の概要
エントリーDOI10.2210/pdb3h5g/pdb
関連するPDBエントリー1coi 1cos 2jgo 3H5F
分子名称COIL SER L16D-Pen, ZINC ION, ACETATE ION, ... (4 entities in total)
機能のキーワードde-novo protein, parallel three-stranded coiled coil, d-penicillamine, de novo protein
タンパク質・核酸の鎖数3
化学式量合計10578.62
構造登録者
Peacock, A.F.A.,Stuckey, J.A.,Pecoraro, V.L. (登録日: 2009-04-22, 公開日: 2009-07-14, 最終更新日: 2023-11-22)
主引用文献Peacock, A.F.,Stuckey, J.A.,Pecoraro, V.L.
Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides.
Angew.Chem.Int.Ed.Engl., 48:7371-7374, 2009
Cited by
PubMed Abstract: The effects of switching the chirality of a single layer of amino acids in a three stranded coiled coil has been investigated. X-ray crystallography reveals that this modification is well tolerated and does not alter the designed structure. In contrast, spectroscopic studies of cadmium binding to both the L- and D- enantiomers of the penicillamine, provide evidence that this switch dramatically alters the metal binding capability, the resulting coordination environment and the position of binding.
PubMed: 19579245
DOI: 10.1002/anie.200902166
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.71 Å)
構造検証レポート
Validation report summary of 3h5g
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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