1gsc

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Current revision (07:26, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1gsc' size='340' side='right'caption='[[1gsc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1gsc' size='340' side='right'caption='[[1gsc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1gsc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1gsc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSC FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=1gsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsc OCA], [https://pdbe.org/1gsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsc RCSB], [https://www.ebi.ac.uk/pdbsum/1gsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsc ProSAT]</span></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=1gsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsc OCA], [https://pdbe.org/1gsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsc RCSB], [https://www.ebi.ac.uk/pdbsum/1gsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
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[https://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1gsc 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=1gsc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Two new crystal forms of isoenzyme 3-3 of rat liver glutathione S-transferase (GST 3-3) have been obtained. They were grown under essentially the same crystallization conditions as those reported for the C2 crystal form [Fu, Rose, Chung, Tam &amp; Wang (1991). Acta Cryst. B47, 813-814]. The new crystals belong to space group P2(1) with one form having cell dimensions a = 101.6, b = 69.5, c = 81.4 A, and beta = 113.6 degrees, and the other form having cell parameters a = 97.4, b = 81.1, c = 69.4 A and beta = 109.2 degrees. These new crystals diffract to at least 2.5 A, resolution. The molecular packing arrangements in these P2(1) crystals have been found by molecular replacement studies.
 
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New crystal forms of a micro-class glutathione S-transferase from rat liver.,Fu JH, Rose J, Tam MF, Wang BC Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):219-24. PMID:15299462<ref>PMID:15299462</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1gsc" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutathione transferase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fu, J H]]
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[[Category: Rattus norvegicus]]
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[[Category: Rose, J P]]
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[[Category: Fu J-H]]
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[[Category: Wang, B C]]
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[[Category: Rose JP]]
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[[Category: Wang B-C]]

Current revision

NEW CRYSTAL FORMS OF A MU CLASS GLUTATHIONE S-TRANSFERASE FROM RAT LIVER

PDB ID 1gsc

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