1p52: Difference between revisions

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[[Image:1p52.gif|left|200px]]<br /><applet load="1p52" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1p52.gif|left|200px]]
caption="1p52, resolution 1.90&Aring;" />
 
'''Structure of Arginine kinase E314D mutant'''<br />
{{Structure
|PDB= 1p52 |SIZE=350|CAPTION= <scene name='initialview01'>1p52</scene>, resolution 1.90&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=DAR:D-ARGININE'>DAR</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3]
|GENE= AK17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6850 Limulus polyphemus])
}}
 
'''Structure of Arginine kinase E314D mutant'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1P52 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus] with <scene name='pdbligand=NO3:'>NO3</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=DAR:'>DAR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P52 OCA].  
1P52 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P52 OCA].  


==Reference==
==Reference==
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase., Pruett PS, Azzi A, Clark SA, Yousef MS, Gattis JL, Somasundaram T, Ellington WR, Chapman MS, J Biol Chem. 2003 Jul 18;278(29):26952-7. Epub 2003 May 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12732621 12732621]
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase., Pruett PS, Azzi A, Clark SA, Yousef MS, Gattis JL, Somasundaram T, Ellington WR, Chapman MS, J Biol Chem. 2003 Jul 18;278(29):26952-7. Epub 2003 May 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12732621 12732621]
[[Category: Arginine kinase]]
[[Category: Arginine kinase]]
[[Category: Limulus polyphemus]]
[[Category: Limulus polyphemus]]
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[[Category: transition state analog]]
[[Category: transition state analog]]


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