1kh5: Difference between revisions

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{{Seed}}
[[Image:1kh5.png|left|200px]]
[[Image:1kh5.png|left|200px]]


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{{STRUCTURE_1kh5|  PDB=1kh5  |  SCENE=  }}  
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===E. COLI ALKALINE PHOSPHATASE MUTANT (D330N) MIMIC OF THE TRANSITION STATES WITH ALUMINIUM FLUORIDE===
===E. COLI ALKALINE PHOSPHATASE MUTANT (D330N) MIMIC OF THE TRANSITION STATES WITH ALUMINIUM FLUORIDE===


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{{ABSTRACT_PUBMED_11884134}}
{{ABSTRACT_PUBMED_11884134}}


==About this Structure==
==About this Structure==
1KH5 is a 2 chains structure of 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=1KH5 OCA].  
[[1kh5]] is a 2 chain structure of [[Alkaline phosphatase]] 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=1KH5 OCA].  
 
==See Also==
*[[Alkaline phosphatase|Alkaline phosphatase]]


==Reference==
==Reference==
<ref group="xtra">PMID:11884134</ref><references group="xtra"/>
<ref group="xtra">PMID:011884134</ref><references group="xtra"/>
[[Category: Alkaline phosphatase]]
[[Category: Alkaline phosphatase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Alkaline phosphatase]]
[[Category: Alkaline phosphatase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:11:00 2009''

Revision as of 12:28, 26 July 2012

File:1kh5.png

Template:STRUCTURE 1kh5

E. COLI ALKALINE PHOSPHATASE MUTANT (D330N) MIMIC OF THE TRANSITION STATES WITH ALUMINIUM FLUORIDE

Template:ABSTRACT PUBMED 11884134

About this Structure

1kh5 is a 2 chain structure of Alkaline phosphatase with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

Reference

  1. Le Du MH, Lamoure C, Muller BH, Bulgakov OV, Lajeunesse E, Menez A, Boulain JC. Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase. J Mol Biol. 2002 Mar 1;316(4):941-53. PMID:11884134 doi:10.1006/jmbi.2001.5384

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