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1EUS

SIALIDASE COMPLEXED WITH 2-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID

1EUS の概要
エントリーDOI10.2210/pdb1eus/pdb
分子名称SIALIDASE, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID (3 entities in total)
機能のキーワードneuraminidase, sialidase, hydrolase
由来する生物種Micromonospora viridifaciens
細胞内の位置Secreted: Q02834
タンパク質・核酸の鎖数1
化学式量合計39183.96
構造登録者
Gaskell, A.,Crennell, S.J.,Taylor, G.L. (登録日: 1996-06-21, 公開日: 1997-01-11, 最終更新日: 2024-02-07)
主引用文献Gaskell, A.,Crennell, S.,Taylor, G.
The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll.
Structure, 3:1197-1205, 1995
Cited by
PubMed Abstract: Sialidases, or neuraminidases, have been implicated in the pathogenesis of many diseases, but are also produced by many non-pathogenic bacteria. Bacterial sialidases are very variable in size, often possessing domains in addition to the catalytic domain. The sialidase from the non-pathogenic soil bacterium Micromonospora viridifaciens is secreted in two forms with molecular weights of 41 kDa or 68 kDa, depending on the nature of the carbohydrate used to induce expression.
PubMed: 8591030
DOI: 10.1016/S0969-2126(01)00255-6
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1eus
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2026-04-08に公開中

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