1vza: Difference between revisions

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[[Image:1vza.gif|left|200px]]<br /><applet load="1vza" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1vza.gif|left|200px]]
caption="1vza, resolution 2.5&Aring;" />
 
'''THYMIDYLATE SYNTHASE E60D MUTANT BINARY COMPLEX WITH 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (DUMP)'''<br />
{{Structure
|PDB= 1vza |SIZE=350|CAPTION= <scene name='initialview01'>1vza</scene>, resolution 2.5&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=UMP:2'-DEOXYURIDINE 5'-MONOPHOSPHATE'>UMP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45]
|GENE= THYMIDYLATE SYNTHASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1582 Lactobacillus casei])
}}
 
'''THYMIDYLATE SYNTHASE E60D MUTANT BINARY COMPLEX WITH 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (DUMP)'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1VZA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei] with <scene name='pdbligand=UMP:'>UMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZA OCA].  
1VZA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZA OCA].  


==Reference==
==Reference==
Entropy in bi-substrate enzymes: proposed role of an alternate site in chaperoning substrate into, and products out of, thymidylate synthase., Birdsall DL, Finer-Moore J, Stroud RM, J Mol Biol. 1996 Jan 26;255(3):522-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8568895 8568895]
Entropy in bi-substrate enzymes: proposed role of an alternate site in chaperoning substrate into, and products out of, thymidylate synthase., Birdsall DL, Finer-Moore J, Stroud RM, J Mol Biol. 1996 Jan 26;255(3):522-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8568895 8568895]
[[Category: Lactobacillus casei]]
[[Category: Lactobacillus casei]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: nucleotide synthase]]
[[Category: nucleotide synthase]]


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