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1A88

CHLOROPEROXIDASE L

1A88 の概要
エントリーDOI10.2210/pdb1a88/pdb
分子名称CHLOROPEROXIDASE L (2 entities in total)
機能のキーワードhaloperoxidase, oxidoreductase
由来する生物種Streptomyces lividans
タンパク質・核酸の鎖数3
化学式量合計89448.62
構造登録者
Hofmann, B.,Toelzer, S.,Pelletier, I.,Altenbuchner, J.,Van Pee, K.-H.,Hecht, H.-J. (登録日: 1998-04-03, 公開日: 1998-10-14, 最終更新日: 2024-05-22)
主引用文献Hofmann, B.,Tolzer, S.,Pelletier, I.,Altenbuchner, J.,van Pee, K.H.,Hecht, H.J.
Structural investigation of the cofactor-free chloroperoxidases.
J.Mol.Biol., 279:889-900, 1998
Cited by
PubMed Abstract: The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites.
PubMed: 9642069
DOI: 10.1006/jmbi.1998.1802
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 1a88
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2026-02-11に公開中

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