1khk: Difference between revisions

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[[Image:1khk.jpg|left|200px]]<br /><applet load="1khk" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1khk.jpg|left|200px]]
caption="1khk, resolution 2.5&Aring;" />
 
'''E. COLI ALKALINE PHOSPHATASE MUTANT (D153HD330N)'''<br />
{{Structure
|PDB= 1khk |SIZE=350|CAPTION= <scene name='initialview01'>1khk</scene>, resolution 2.5&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1]
|GENE=
}}
 
'''E. COLI ALKALINE PHOSPHATASE MUTANT (D153HD330N)'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1KHK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KHK OCA].  
1KHK is a [[Single protein]] 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=1KHK OCA].  


==Reference==
==Reference==
Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase., Le Du MH, Lamoure C, Muller BH, Bulgakov OV, Lajeunesse E, Menez A, Boulain JC, J Mol Biol. 2002 Mar 1;316(4):941-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11884134 11884134]
Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase., Le Du MH, Lamoure C, Muller BH, Bulgakov OV, Lajeunesse E, Menez A, Boulain JC, J Mol Biol. 2002 Mar 1;316(4):941-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11884134 11884134]
[[Category: Alkaline phosphatase]]
[[Category: Alkaline phosphatase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: hydrolase]]
[[Category: hydrolase]]


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