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5AEC

Type II Baeyer-Villiger monooxygenase.The oxygenating constituent of 3,6-diketocamphane monooxygenase from CAM plasmid of Pseudomonas putida in complex with FMN.

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5AEC の概要
エントリーDOI10.2210/pdb5aec/pdb
分子名称3,6-DIKETOCAMPHANE 1,6 MONOOXYGENASE, PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID), GLYCEROL, ... (6 entities in total)
機能のキーワードoxidoreductase, biocatalysis, flavin monooxygenase
由来する生物種PSEUDOMONAS PUTIDA
タンパク質・核酸の鎖数2
化学式量合計86869.51
構造登録者
主引用文献Isupov, M.N.,Schroder, E.,Gibson, R.P.,Beecher, J.,Donadio, G.,Saneei, V.,Dcunha, S.A.,Mcghie, E.J.,Sayer, C.,Davenport, C.F.,Lau, P.C.,Hasegawa, Y.,Iwaki, H.,Kadow, M.,Balke, K.,Bornscheuer, U.T.,Bourenkov, G.,Littlechild, J.A.
The Oxygenating Constituent of 3,6-Diketocamphane Monooxygenase from the Cam Plasmid of Pseudomonas Putida: The First Crystal Structure of a Type II Baeyer-Villiger Monooxygenase.
Acta Crystallogr.,Sect.D, 71:2344-, 2015
Cited by
PubMed Abstract: The three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer-Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 Å resolution. The structure of this dimeric FMN-dependent enzyme, which is encoded on the large CAM plasmid of Pseudomonas putida, has been solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model. The orientation of the isoalloxazine ring of the FMN cofactor in the active site of this TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a β-bulge at the C-terminus of β-strand 3, which is a feature observed in many proteins of this superfamily.
PubMed: 26527149
DOI: 10.1107/S1399004715017939
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.93 Å)
構造検証レポート
Validation report summary of 5aec
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2026-01-28に公開中

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