1ix6: Difference between revisions

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[[Image:1ix6.gif|left|200px]]<br /><applet load="1ix6" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ix6.gif|left|200px]]
caption="1ix6, resolution 2.2&Aring;" />
 
'''Aspartate Aminotransferase Active Site Mutant V39F'''<br />
{{Structure
|PDB= 1ix6 |SIZE=350|CAPTION= <scene name='initialview01'>1ix6</scene>, resolution 2.2&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1]
|GENE=
}}
 
'''Aspartate Aminotransferase Active Site Mutant V39F'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1IX6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX6 OCA].  
1IX6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX6 OCA].  


==Reference==
==Reference==
Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis., Hayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H, J Biol Chem. 2003 Mar 14;278(11):9481-8. Epub 2002 Dec 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12488449 12488449]
Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis., Hayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H, J Biol Chem. 2003 Mar 14;278(11):9481-8. Epub 2002 Dec 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12488449 12488449]
[[Category: Aspartate transaminase]]
[[Category: Aspartate transaminase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: active site mutant]]
[[Category: active site mutant]]


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