1wnv: Difference between revisions

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


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===D136A mutant of Heme Oxygenase from Corynebacterium diphtheriae (HmuO)===
===D136A mutant of Heme Oxygenase from Corynebacterium diphtheriae (HmuO)===


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{{ABSTRACT_PUBMED_15528205}}


==About this Structure==
==About this Structure==
1WNV is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNV OCA].  
[[1wnv]] is a 3 chain structure of [[Heme oxygenase]] with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNV OCA].  
 
==See Also==
*[[Heme oxygenase|Heme oxygenase]]


==Reference==
==Reference==
<ref group="xtra">PMID:15528205</ref><references group="xtra"/>
<ref group="xtra">PMID:015528205</ref><references group="xtra"/>
[[Category: Corynebacterium diphtheriae]]
[[Category: Corynebacterium diphtheriae]]
[[Category: Heme oxygenase]]
[[Category: Heme oxygenase]]
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[[Category: Alpha-helix]]
[[Category: Alpha-helix]]
[[Category: Heme]]
[[Category: Heme]]
 
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:38:20 2009''

Revision as of 13:34, 25 July 2012

File:1wnv.png

Template:STRUCTURE 1wnv

D136A mutant of Heme Oxygenase from Corynebacterium diphtheriae (HmuO)

Template:ABSTRACT PUBMED 15528205

About this Structure

1wnv is a 3 chain structure of Heme oxygenase with sequence from Corynebacterium diphtheriae. Full crystallographic information is available from OCA.

See Also

Reference

  1. Matsui T, Furukawa M, Unno M, Tomita T, Ikeda-Saito M. Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism. J Biol Chem. 2005 Jan 28;280(4):2981-9. Epub 2004 Nov 4. PMID:15528205 doi:10.1074/jbc.M410263200

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