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3A33

UbcH5b~Ubiquitin Conjugate

3A33 の概要
エントリーDOI10.2210/pdb3a33/pdb
関連するPDBエントリー1UBQ 2ESK
分子名称Ubiquitin-conjugating enzyme E2 D2, Ubiquitin, GLYCEROL, ... (4 entities in total)
機能のキーワードe2 ubiquitin-conjugating enzyme, ubiquitin, ligase, ubl conjugation pathway, isopeptide bond, nucleus
由来する生物種Homo sapiens (human)
詳細
タンパク質・核酸の鎖数2
化学式量合計25623.30
構造登録者
Sakata, E.,Satoh, T.,Yamamoto, S.,Yamaguchi, Y.,Yagi-Utsumi, M.,Kurimoto, E.,Wakatsuki, S.,Kato, K. (登録日: 2009-06-08, 公開日: 2009-11-24, 最終更新日: 2024-11-06)
主引用文献Sakata, E.,Satoh, T.,Yamamoto, S.,Yamaguchi, Y.,Yagi-Utsumi, M.,Kurimoto, E.,Tanaka, K.,Wakatsuki, S.,Kato, K.
Crystal Structure of UbcH5b~Ubiquitin Intermediate: Insight into the Formation of the Self-Assembled E2~Ub Conjugates
Structure, 18:138-147, 2010
Cited by
PubMed Abstract: E2 ubiquitin-conjugating enzymes catalyze the attachment of ubiquitin to lysine residues of target proteins. The UbcH5b E2 enzyme has been shown to play a key role in the initiation of the ubiquitination of substrate proteins upon action of several E3 ligases. Here we have determined the 2.2 A crystal structure of an intermediate of UbcH5b~ubiquitin (Ub) conjugate, which is assembled into an infinite spiral through the backside interaction. This active complex may provide multiple E2 active sites, enabling efficient ubiquitination of substrates. Indeed, biochemical assays support a model in which the self-assembled UbcH5b~Ub can serve as a bridge for the gap between the lysine residue of the substrate and the catalytic cysteine of E2.
PubMed: 20152160
DOI: 10.1016/j.str.2009.11.007
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 3a33
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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