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1V35

Crystal Structure of Eoyl-ACP Reductase with NADH

1V35 の概要
エントリーDOI10.2210/pdb1v35/pdb
関連するPDBエントリー1UH5
分子名称enoyl-ACP reductase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE (3 entities in total)
機能のキーワードfabi, nadh, enoyl-acp reductase, p.falciparum, oxidoreductase
由来する生物種Plasmodium falciparum (malaria parasite P. falciparum)
タンパク質・核酸の鎖数2
化学式量合計75819.25
構造登録者
SwarnaMukhi, P.L.,Kapoor, M.,surolia, N.,Surolia, A.,Suguna, K. (登録日: 2003-10-28, 公開日: 2004-09-28, 最終更新日: 2023-10-25)
主引用文献Pidugu, L.S.,Kapoor, M.,Surolia, N.,Surolia, A.,Suguna, K.
Structural basis for the variation in triclosan affinity to enoyl reductases.
J.Mol.Biol., 343:147-155, 2004
Cited by
PubMed Abstract: Bacteria synthesize fatty acids in a dissociated type pathway different from that in humans. Enoyl acyl carrier protein reductase, which catalyzes the final step of fatty acid elongation, has been validated as a potential anti-microbial drug target. Triclosan is known to inhibit this enzyme effectively. Precise characterization of the mode of triclosan binding is required to develop highly specific inhibitors. With this in view, interactions between triclosan, the cofactor NADH/NAD+ and the enzyme from five different species, one plant and four of microbial origin, have been examined in the available crystal structures. A comparison of these structures shows major structural differences at the substrate/inhibitor/cofactor-binding loop. The analysis reveals that the conformation of this flexible loop and the binding affinities of triclosan to each of these enzymes are strongly correlated.
PubMed: 15381426
DOI: 10.1016/j.jmb.2004.08.033
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 1v35
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2025-07-30に公開中

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