2acu: Difference between revisions

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[[Image:2acu.png|left|200px]]


{{STRUCTURE_2acu|  PDB=2acu  |  SCENE=  }}
==TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRATE STEREOCHEMICAL SELECTIVITY IN THE REDUCTION REACTION OF HUMAN ALDOSE REDUCTASE: ENZYME KINETICS AND THE CRYSTAL STRUCTURE OF THE Y48H MUTANT ENZYME==
 
<StructureSection load='2acu' size='340' side='right'caption='[[2acu]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
===TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRATE STEREOCHEMICAL SELECTIVITY IN THE REDUCTION REACTION OF HUMAN ALDOSE REDUCTASE: ENZYME KINETICS AND THE CRYSTAL STRUCTURE OF THE Y48H MUTANT ENZYME===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2acu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ACU FirstGlance]. <br>
{{ABSTRACT_PUBMED_8117659}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2acu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2acu OCA], [https://pdbe.org/2acu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2acu RCSB], [https://www.ebi.ac.uk/pdbsum/2acu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2acu ProSAT]</span></td></tr>
[[2acu]] is a 1 chain structure of [[Aldose Reductase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACU OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
== 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/ac/2acu_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=2acu ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Aldose Reductase|Aldose Reductase]]
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:008117659</ref><references group="xtra"/>
[[Category: Aldehyde reductase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bohren, K M.]]
[[Category: Large Structures]]
[[Category: Gabbay, K H.]]
[[Category: Bohren KM]]
[[Category: Grimshaw, C E.]]
[[Category: Gabbay KH]]
[[Category: Harrison, D H.]]
[[Category: Grimshaw CE]]
[[Category: Lai, C J.]]
[[Category: Harrison DH]]
[[Category: Petsko, G A.]]
[[Category: Lai C-J]]
[[Category: Ringe, D.]]
[[Category: Petsko GA]]
[[Category: Oxidoreductase]]
[[Category: Ringe D]]

Latest revision as of 09:12, 14 February 2024

TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRATE STEREOCHEMICAL SELECTIVITY IN THE REDUCTION REACTION OF HUMAN ALDOSE REDUCTASE: ENZYME KINETICS AND THE CRYSTAL STRUCTURE OF THE Y48H MUTANT ENZYME

2acu, resolution 1.76Å

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