1asa

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==THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE==
==THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE==
<StructureSection load='1asa' size='340' side='right' caption='[[1asa]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1asa' size='340' side='right' caption='[[1asa]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAE:MALEIC+ACID'>MAE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAE:MALEIC+ACID'>MAE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1asa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1asa OCA], [http://pdbe.org/1asa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1asa RCSB], [http://www.ebi.ac.uk/pdbsum/1asa PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1asa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1asa OCA], [http://pdbe.org/1asa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1asa RCSB], [http://www.ebi.ac.uk/pdbsum/1asa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1asa ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1asa ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1asa ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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==See Also==
 
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*[[Aspartate Aminotransferase|Aspartate Aminotransferase]]
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 10:46, 15 November 2017

THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE

1asa, resolution 2.40Å

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