2gtu: Difference between revisions

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[[Image:2gtu.gif|left|200px]]<br /><applet load="2gtu" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2gtu.gif|left|200px]]
caption="2gtu, resolution 2.55&Aring;" />
 
'''LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORM'''<br />
{{Structure
|PDB= 2gtu |SIZE=350|CAPTION= <scene name='initialview01'>2gtu</scene>, resolution 2.55&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18]
|GENE= GSTM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORM'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2GTU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GTU OCA].  
2GTU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GTU OCA].  


==Reference==
==Reference==
The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases., Patskovsky YV, Patskovska LN, Listowsky I, J Biol Chem. 2000 Feb 4;275(5):3296-304. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10652317 10652317]
The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases., Patskovsky YV, Patskovska LN, Listowsky I, J Biol Chem. 2000 Feb 4;275(5):3296-304. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10652317 10652317]
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: transferase]]
[[Category: transferase]]


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