1wx2: Difference between revisions

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{{Seed}}
[[Image:1wx2.png|left|200px]]
[[Image:1wx2.png|left|200px]]


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==About this Structure==
==About this Structure==
1WX2 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_castaneoglobisporus Streptomyces castaneoglobisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WX2 OCA].  
[[1wx2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_castaneoglobisporus Streptomyces castaneoglobisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WX2 OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:16436386</ref><references group="xtra"/>
<ref group="xtra">PMID:016436386</ref><references group="xtra"/>
[[Category: Monophenol monooxygenase]]
[[Category: Monophenol monooxygenase]]
[[Category: Streptomyces castaneoglobisporus]]
[[Category: Streptomyces castaneoglobisporus]]
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[[Category: Copper transfer]]
[[Category: Copper transfer]]
[[Category: Dioxygen]]
[[Category: Dioxygen]]
[[Category: Oxidoreductase-metal transport complex]]
[[Category: Type-3 copper]]
[[Category: Type-3 copper]]
[[Category: Tyrosinase]]
[[Category: Tyrosinase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:43:22 2009''

Revision as of 09:53, 16 November 2011

File:1wx2.png

Template:STRUCTURE 1wx2

Crystal Structure of the oxy-form of the copper-bound Streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein prepared by the addition of hydrogenperoxide

Template:ABSTRACT PUBMED 16436386

About this Structure

1wx2 is a 2 chain structure with sequence from Streptomyces castaneoglobisporus. Full crystallographic information is available from OCA.

Reference

  1. Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M. Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J Biol Chem. 2006 Mar 31;281(13):8981-90. Epub 2006 Jan 25. PMID:16436386 doi:10.1074/jbc.M509785200

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