1ah4: Difference between revisions

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[[Image:1ah4.png|left|200px]]


{{STRUCTURE_1ah4|  PDB=1ah4  |  SCENE=  }}
==PIG ALDOSE REDUCTASE, HOLO FORM==
 
<StructureSection load='1ah4' size='340' side='right'caption='[[1ah4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
===PIG ALDOSE REDUCTASE, HOLO FORM===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1ah4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AH4 FirstGlance]. <br>
{{ABSTRACT_PUBMED_9195881}}
</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&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</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=1ah4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ah4 OCA], [https://pdbe.org/1ah4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ah4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ah4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ah4 ProSAT]</span></td></tr>
[[1ah4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH4 OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALDR_PIG ALDR_PIG] 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/ah/1ah4_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=1ah4 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Aldose Reductase|Aldose Reductase]]
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]]
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
==Reference==
__TOC__
<ref group="xtra">PMID:009195881</ref><references group="xtra"/>
</StructureSection>
[[Category: Aldehyde reductase]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Moras, D.]]
[[Category: Moras D]]
[[Category: Podjarny, A.]]
[[Category: Podjarny A]]
[[Category: Aldose reductase]]
[[Category: Diabetes]]
[[Category: Inhibition]]
[[Category: Oxidoreductase]]

Latest revision as of 18:24, 13 March 2024

PIG ALDOSE REDUCTASE, HOLO FORMPIG ALDOSE REDUCTASE, HOLO FORM

Structural highlights

1ah4 is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALDR_PIG 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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ah4, resolution 2.00Å

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