1W6C

AGAO holoenzyme in a small cell, at 2.2 angstroms

1W6C の概要

• エントリーDOI: 10.2210/pdb1w6c/pdb
• 関連するPDBエントリー: 1W5Z 1W6G
• 分子名称: PHENYLETHYLAMINE OXIDASE, COPPER (II) ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, amine oxidase, copper containing, metal-binding, tpq, quinone, holoenzyme
• 由来する生物種: ARTHROBACTER GLOBIFORMIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 71913.85

構造登録者

Duff, A.P.,Langley, D.B.,Juda, G.A.,Shepard, E.M.,Dooley, D.M.,Freeman, H.C.,Guss, J.M. (登録日: 2004-08-17, 公開日: 2005-12-08, 最終更新日: 2023-12-13)

主引用文献

Langley, D.B.,Duff, A.P.,Freeman, H.C.,Guss, J.M.
The Copper Containing Amine Oxidase from Arthrobacter Globiformis: Refinement at 1.55 And 2.20 A Resolution in Two Crystal Forms.
Acta Crystallogr.,Sect.F, 62:1052-, 2006

PubMed Abstract: Copper-containing amine oxidases are found in all the major kingdoms of life. They catalyse the oxidation of organic amines in the presence of molecular dioxygen to aldehydes and hydrogen peroxide. The catalytic centres contain a Cu atom and a topaquinone cofactor formed autocatalytically from a tyrosine residue in the presence of Cu and molecular oxygen. The structure of the Cu-containing amine oxidase from Arthrobacter globiformis, which was previously refined at 1.8 A resolution in space group C2 with unit-cell parameters a = 157.84, b = 63.24, c = 91.98 A, beta = 112.0 degrees [Wilce et al. (1997), Biochemistry, 36, 16116-16133], has been re-refined with newly recorded data at 1.55 A resolution. The structure has also been solved and refined at 2.2 A resolution in a new crystal form, space group C2, with unit-cell parameters a = 158.04, b = 64.06, c = 69.69 A, beta = 111.7 degrees.

PubMed: 17077478
DOI: 10.1107/S1744309106038814

実験手法

X-RAY DIFFRACTION (2.2 Å)