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< | ==THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE== | ||
<StructureSection load='1asb' size='340' side='right'caption='[[1asb]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1asb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ASB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAE:MALEIC+ACID'>MAE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1asb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1asb OCA], [https://pdbe.org/1asb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1asb RCSB], [https://www.ebi.ac.uk/pdbsum/1asb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1asb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/as/1asb_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1asb ConSurf]. | |||
<div style="clear:both"></div> | |||
== | ==See Also== | ||
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ringe D]] | ||
[[Category: | [[Category: Schumacher C]] | ||
Latest revision as of 18:27, 13 March 2024
THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASETHE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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