1W6C

AGAO holoenzyme in a small cell, at 2.2 angstroms

Summary for 1W6C

• Entry DOI: 10.2210/pdb1w6c/pdb
• Related: 1W5Z 1W6G
• Descriptor: PHENYLETHYLAMINE OXIDASE, COPPER (II) ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, amine oxidase, copper containing, metal-binding, tpq, quinone, holoenzyme
• Biological source: ARTHROBACTER GLOBIFORMIS
• Total number of polymer chains: 1
• Total formula weight: 71913.85

Authors

Duff, A.P.,Langley, D.B.,Juda, G.A.,Shepard, E.M.,Dooley, D.M.,Freeman, H.C.,Guss, J.M. (deposition date: 2004-08-17, release date: 2005-12-08, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)