2aaq: Difference between revisions

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==Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI==
==Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI==
<StructureSection load='2aaq' size='340' side='right' caption='[[2aaq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='2aaq' size='340' side='right' caption='[[2aaq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hGR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hGR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </span></td></tr>
<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=2aaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aaq OCA], [http://pdbe.org/2aaq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aaq RCSB], [http://www.ebi.ac.uk/pdbsum/2aaq PDBsum]</span></td></tr>
<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=2aaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aaq OCA], [http://pdbe.org/2aaq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aaq RCSB], [http://www.ebi.ac.uk/pdbsum/2aaq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2aaq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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=2aaq ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Glutathione Reductase|Glutathione Reductase]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 11:24, 12 October 2017

Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPICrystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI

Structural highlights

2aaq is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , ,
Gene:hGR (HUMAN)
Activity:Glutathione-disulfide reductase, with EC number 1.8.1.7
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GSHR_HUMAN] Maintains high levels of reduced glutathione in the cytosol.

Evolutionary Conservation

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

2aaq, resolution 2.60Å

Drag the structure with the mouse to rotate

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