1ege

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[[Image:1ege.png|left|200px]]
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{{STRUCTURE_1ege| PDB=1ege | SCENE= }}
{{STRUCTURE_1ege| PDB=1ege | SCENE= }}
===STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE===
===STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE===
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{{ABSTRACT_PUBMED_8823176}}
{{ABSTRACT_PUBMED_8823176}}
==About this Structure==
==About this Structure==
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1EGE is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGE OCA].
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[[1ege]] is a 4 chain structure of [[Acyl-CoA dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGE OCA].
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==See Also==
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*[[Acyl-CoA dehydrogenase|Acyl-CoA dehydrogenase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:8823176</ref><references group="xtra"/>
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<ref group="xtra">PMID:008823176</ref><references group="xtra"/>
[[Category: Acyl-CoA dehydrogenase]]
[[Category: Acyl-CoA dehydrogenase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Electron transfer]]
[[Category: Electron transfer]]
[[Category: Flavoprotein]]
[[Category: Flavoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:00:32 2009''
 

Revision as of 14:23, 27 July 2012

Template:STRUCTURE 1ege

Contents

STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE

Template:ABSTRACT PUBMED 8823176

About this Structure

1ege is a 4 chain structure of Acyl-CoA dehydrogenase with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ. Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. Biochemistry. 1996 Sep 24;35(38):12412-20. PMID:8823176 doi:10.1021/bi9607867

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