1yoo: Difference between revisions

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[[Image:1yoo.jpg|left|200px]]<br /><applet load="1yoo" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1yoo.jpg|left|200px]]
caption="1yoo, resolution 2.40&Aring;" />
 
'''ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID'''<br />
{{Structure
|PDB= 1yoo |SIZE=350|CAPTION= <scene name='initialview01'>1yoo</scene>, resolution 2.40&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=IVA:ISOVALERIC ACID'>IVA</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 MUTANT ATB17 WITH ISOVALERIC ACID'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1YOO 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> and <scene name='pdbligand=IVA:'>IVA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1YOO OCA].  
1YOO 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=1YOO OCA].  


==Reference==
==Reference==
Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues., Oue S, Okamoto A, Yano T, Kagamiyama H, J Biol Chem. 1999 Jan 22;274(4):2344-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9891001 9891001]
Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues., Oue S, Okamoto A, Yano T, Kagamiyama H, J Biol Chem. 1999 Jan 22;274(4):2344-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9891001 9891001]
[[Category: Aspartate transaminase]]
[[Category: Aspartate transaminase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: aminotransferase]]
[[Category: aminotransferase]]


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