1vjc: Difference between revisions

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[[Image:1vjc.gif|left|200px]]<br /><applet load="1vjc" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1vjc.gif|left|200px]]
caption="1vjc, resolution 2.1&Aring;" />
 
'''Structure of pig muscle PGK complexed with MgATP'''<br />
{{Structure
|PDB= 1vjc |SIZE=350|CAPTION= <scene name='initialview01'>1vjc</scene>, resolution 2.1&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3]
|GENE=
}}
 
'''Structure of pig muscle PGK complexed with MgATP'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1VJC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJC OCA].  
1VJC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJC OCA].  


==Reference==
==Reference==
Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP., Flachner B, Kovari Z, Varga A, Gugolya Z, Vonderviszt F, Naray-Szabo G, Vas M, Biochemistry. 2004 Mar 30;43(12):3436-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15035615 15035615]
Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP., Flachner B, Kovari Z, Varga A, Gugolya Z, Vonderviszt F, Naray-Szabo G, Vas M, Biochemistry. 2004 Mar 30;43(12):3436-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15035615 15035615]
[[Category: Phosphoglycerate kinase]]
[[Category: Phosphoglycerate kinase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: mg]]
[[Category: mg]]


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