1p50: Difference between revisions

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[[Image:1p50.gif|left|200px]]<br /><applet load="1p50" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1p50.gif|left|200px]]
caption="1p50, resolution 2.8&Aring;" />
 
'''Transition state structure of an Arginine Kinase mutant'''<br />
{{Structure
|PDB= 1p50 |SIZE=350|CAPTION= <scene name='initialview01'>1p50</scene>, resolution 2.8&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=NO3:NITRATE ION'>NO3</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=
}}
 
'''Transition state structure of an Arginine Kinase mutant'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1P50 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=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=NO3:'>NO3</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=1P50 OCA].  
1P50 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=1P50 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]]
[[Category: transition state]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:19:57 2008''
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