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1EDO

THE X-RAY STRUCTURE OF BETA-KETO ACYL CARRIER PROTEIN REDUCTASE FROM BRASSICA NAPUS COMPLEXED WITH NADP+

1EDO の概要
エントリーDOI10.2210/pdb1edo/pdb
分子名称BETA-KETO ACYL CARRIER PROTEIN REDUCTASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
機能のキーワードnucleotide fold, rossmann fold, oxidoreductase
由来する生物種Brassica napus (rape)
細胞内の位置Plastid, chloroplast (By similarity): Q93X62
タンパク質・核酸の鎖数1
化学式量合計26102.82
構造登録者
Fisher, M.,Kroon, J.T.,Martindale, W.,Stuitje, A.R.,Slabas, A.R.,Rafferty, J.B. (登録日: 2000-01-28, 公開日: 2001-01-31, 最終更新日: 2024-02-07)
主引用文献Fisher, M.,Kroon, J.T.,Martindale, W.,Stuitje, A.R.,Slabas, A.R.,Rafferty, J.B.
The X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.
Structure Fold.Des., 8:339-347, 2000
Cited by
PubMed Abstract: beta-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family.
PubMed: 10801480
DOI: 10.1016/S0969-2126(00)00115-5
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 1edo
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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