1knr

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[[Image:1knr.png|left|200px]]
[[Image:1knr.png|left|200px]]
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{{STRUCTURE_1knr| PDB=1knr | SCENE= }}
{{STRUCTURE_1knr| PDB=1knr | SCENE= }}
===L-aspartate oxidase: R386L mutant===
===L-aspartate oxidase: R386L mutant===
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{{ABSTRACT_PUBMED_11863440}}
{{ABSTRACT_PUBMED_11863440}}
==About this Structure==
==About this Structure==
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1KNR is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNR OCA].
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[[1knr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNR OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:11863440</ref><references group="xtra"/>
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<ref group="xtra">PMID:011863440</ref><ref group="xtra">PMID:018774824</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: L-aspartate oxidase]]
[[Category: L-aspartate oxidase]]
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[[Category: Mattevi, A.]]
[[Category: Mattevi, A.]]
[[Category: Fumarate reductase family of oxidoreductase]]
[[Category: Fumarate reductase family of oxidoreductase]]
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[[Category: Oxidoreductase]]
[[Category: Succinate dehydrogenase]]
[[Category: Succinate dehydrogenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:27:08 2009''
 

Revision as of 20:39, 5 December 2012

Template:STRUCTURE 1knr

L-aspartate oxidase: R386L mutant

Template:ABSTRACT PUBMED 11863440

About this Structure

1knr is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Bossi RT, Negri A, Tedeschi G, Mattevi A. Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis. Biochemistry. 2002 Mar 5;41(9):3018-24. PMID:11863440
  • Blasiak LC, Drennan CL. Structural perspective on enzymatic halogenation. Acc Chem Res. 2009 Jan 20;42(1):147-55. PMID:18774824 doi:10.1021/ar800088r

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