2pvq: Difference between revisions

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[[Image:2pvq.jpg|left|200px]]<br /><applet load="2pvq" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2pvq.jpg|left|200px]]
caption="2pvq, resolution 1.803&Aring;" />
 
'''Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site'''<br />
{{Structure
|PDB= 2pvq |SIZE=350|CAPTION= <scene name='initialview01'>2pvq</scene>, resolution 1.803&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene>
|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= gst ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=529 Ochrobactrum anthropi])
}}
 
'''Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2PVQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GTT:'>GTT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2PVQ OCA].  
2PVQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVQ OCA].  


==Reference==
==Reference==
Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site., Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C, Proteins. 2007 Dec 12;71(1):16-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18076047 18076047]
Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site., Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C, Proteins. 2007 Dec 12;71(1):16-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18076047 18076047]
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Ochrobactrum anthropi]]
[[Category: Ochrobactrum anthropi]]
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[[Category: xenobiotics detoxification]]
[[Category: xenobiotics detoxification]]


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