2xfw

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[[Image:2xfw.png|left|200px]]
[[Image:2xfw.png|left|200px]]
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{{STRUCTURE_2xfw| PDB=2xfw | SCENE= }}
{{STRUCTURE_2xfw| PDB=2xfw | SCENE= }}
===STRUCTURE OF THE E192N MUTANT OF E. COLI N-ACETYLNEURAMINIC ACID LYASE IN COMPLEX WITH PYRUVATE IN CRYSTAL FORM II===
===STRUCTURE OF THE E192N MUTANT OF E. COLI N-ACETYLNEURAMINIC ACID LYASE IN COMPLEX WITH PYRUVATE IN CRYSTAL FORM II===
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{{ABSTRACT_PUBMED_20826162}}
{{ABSTRACT_PUBMED_20826162}}
==About this Structure==
==About this Structure==
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2XFW is a 4 chains structure with sequences 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=2XFW OCA].
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[[2xfw]] is a 4 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=2XFW OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:20826162</ref><references group="xtra"/>
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<ref group="xtra">PMID:020826162</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: N-acetylneuraminate lyase]]
[[Category: N-acetylneuraminate lyase]]
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[[Category: Trinh, C H.]]
[[Category: Trinh, C H.]]
[[Category: Lyase]]
[[Category: Lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Nov 18 00:21:48 2010''
 

Revision as of 20:26, 7 January 2013

Template:STRUCTURE 2xfw

STRUCTURE OF THE E192N MUTANT OF E. COLI N-ACETYLNEURAMINIC ACID LYASE IN COMPLEX WITH PYRUVATE IN CRYSTAL FORM II

Template:ABSTRACT PUBMED 20826162

About this Structure

2xfw is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Campeotto I, Bolt AH, Harman TA, Dennis C, Trinh CH, Phillips SE, Nelson A, Pearson AR, Berry A. Structural Insights into Substrate Specificity in Variants of N-Acetylneuraminic Acid Lyase Produced by Directed Evolution. J Mol Biol. 2010 Sep 6. PMID:20826162 doi:10.1016/j.jmb.2010.08.008

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