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1IR7

IM mutant of lysozyme

1IR7 の概要
エントリーDOI10.2210/pdb1ir7/pdb
関連するPDBエントリー1IR8 1IR9
分子名称lysozyme (2 entities in total)
機能のキーワードhydrolase, egg white
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14349.20
構造登録者
Ohmura, T.,Ueda, T.,Hashimoto, Y.,Imoto, T. (登録日: 2001-09-19, 公開日: 2001-10-03, 最終更新日: 2024-10-16)
主引用文献Ohmura, T.,Ueda, T.,Hashimoto, Y.,Imoto, T.
Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme.
Protein Eng., 14:421-425, 2001
Cited by
PubMed Abstract: X-ray structure determination of proteins by using the multiple-wavelength anomalous dispersion method targeting selenomethionine is now widely employed. Isoleucine was examined for the second choice of the substitution of methionine next to leucine. We performed a systematic mutational study of the substitutions of methionine for isoleucine. All mutated lysozymes were less stable than the wild-type by about 1 kcal/mol and it is suggested that this instability was caused by the change in residual hydrophobicity from isoleucine to methionine. The X-ray structures of all mutant lysozymes were very similar to that of the wild-type. In addition, both the accessible surface areas and the conformation of the side chain of methionine in all mutant lysozymes were similar to those of the side chain at the respective isoleucine in the wild-type. Therefore, it is suggested that the mutation from isoleucine to methionine in a protein can be considered as a "safe" substitution.
PubMed: 11477222
DOI: 10.1093/protein/14.6.421
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 1ir7
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2026-04-15に公開中

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