2l5h: Difference between revisions

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[[Image:2l5h.jpg|left|200px]]
[[Image:2l5h.png|left|200px]]


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==About this Structure==
==About this Structure==
[[2l5h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5H OCA].  
[[2l5h]] is a 2 chain structure of [[Phosphotransferase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5H OCA].  
 
==See Also==
*[[Phosphotransferase|Phosphotransferase]]


==Reference==
==Reference==
<ref group="xtra">PMID:21162528</ref><references group="xtra"/>
<ref group="xtra">PMID:021162528</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Phosphoenolpyruvate--protein phosphotransferase]]
[[Category: Phosphoenolpyruvate--protein phosphotransferase]]
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[[Category: Schwieters, C D.]]
[[Category: Schwieters, C D.]]
[[Category: Takayama, Y D.]]
[[Category: Takayama, Y D.]]
[[Category: Dimer]]
[[Category: Protein]]
[[Category: Transferase]]

Revision as of 11:29, 25 April 2012

File:2l5h.png

Template:STRUCTURE 2l5h

Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray ScatteringSolution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering

Template:ABSTRACT PUBMED 21162528

About this StructureAbout this Structure

2l5h is a 2 chain structure of Phosphotransferase with sequence from Escherichia coli. Full experimental information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. Takayama Y, Schwieters CD, Grishaev A, Ghirlando R, Clore GM. Combined Use of Residual Dipolar Couplings and Solution X-ray Scattering To Rapidly Probe Rigid-Body Conformational Transitions in a Non-phosphorylatable Active-Site Mutant of the 128 kDa Enzyme I Dimer. J Am Chem Soc. 2010 Dec 16. PMID:21162528 doi:10.1021/ja109866w

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