Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1EK4

BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEX WITH DODECANOIC ACID TO 1.85 RESOLUTION

1EK4 の概要
エントリーDOI10.2210/pdb1ek4/pdb
関連するPDBエントリー1dd8
分子名称BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I, LAURIC ACID (3 entities in total)
機能のキーワードfatty acid synthase, thiolase fold, claisen condensation, fatty acid substrate complex, transferase
由来する生物種Escherichia coli
細胞内の位置Cytoplasm: P0A953
タンパク質・核酸の鎖数4
化学式量合計177096.10
構造登録者
Olsen, J.G.,Kadziola, A.,Siggaard-Andersen, M.,von Wettstein-Knowles, P.,Larsen, S. (登録日: 2000-03-06, 公開日: 2001-04-11, 最終更新日: 2024-10-30)
主引用文献Olsen, J.G.,Kadziola, A.,von Wettstein-Knowles, P.,Siggaard-Andersen, M.,Larsen, S.
Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery.
Structure, 9:233-243, 2001
Cited by
PubMed Abstract: beta-ketoacyl-acyl carrier protein synthase (KAS) I is vital for the construction of the unsaturated fatty acid carbon skeletons characterizing E. coli membrane lipids. The new carbon-carbon bonds are created by KAS I in a Claisen condensation performed in a three-step enzymatic reaction. KAS I belongs to the thiolase fold enzymes, of which structures are known for five other enzymes.
PubMed: 11286890
DOI: 10.1016/S0969-2126(01)00583-4
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.85 Å)
構造検証レポート
Validation report summary of 1ek4
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

PDB statisticsPDBj update infoContact PDBjnumon