1glp - Revision history

OCA at 07:25, 7 February 2024

OCA — Wed, 07 Feb 2024 07:25:31 GMT

←Older revision		Revision as of 07:25, 7 February 2024
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	<StructureSection load='1glp' size='340' side='right'caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1glp' size='340' side='right'caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GLP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GLP FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.9Å</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>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [https://pdbe.org/1glp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [https://www.ebi.ac.uk/pdbsum/1glp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1glp 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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [https://pdbe.org/1glp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [https://www.ebi.ac.uk/pdbsum/1glp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1glp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GSTP1_MOUSE GSTP1_MOUSE]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity).	+	[https://www.uniprot.org/uniprot/GSTP1_MOUSE GSTP1_MOUSE] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity).
	== 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=1glp 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=1glp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The three-dimensional crystal structure of pi class glutathione S-transferase YfYf from mouse liver complexed with the inhibitor S-(p-nitrobenzyl)glutathione has been determined at 1.8 A resolution by X-ray diffraction. In addition two complexes with glutathione sulphonic acid and S-hexylglutathione have been determined at resolutions of 1.9 and 2.2 A, respectively. The high resolution of the S-(p-nitrobenzyl)glutathione complex allows a detailed analysis of the active site including the hydrophobic (H-) subsite. The nitrobenzyl moiety occupies a hydrophobic pocket with its aromatic ring sandwiched between Phe8 and the hydroxyl group of Tyr108. An insertion of two residues Gly41 and Leu42, with respect to the pig enzyme, splits helix alpha B into an alpha-helix and a 3(10) helix. Water bridges between carbonyl oxygen atoms of the alpha-helix at its C terminus and the amide NH groups of the 3(10) helix at its N terminus provide structural continuity between these two secondary elements. Tyr7 appears to be the only residue close to the sulphur atom of glutathione, while three conserved water molecules lie in the surrounding area in all complexes. The enzyme mechanism is discussed on the basis of the structural analysis.
-
-	Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors.,Garcia-Saez I, Parraga A, Phillips MF, Mantle TJ, Coll M J Mol Biol. 1994 Apr 1;237(3):298-314. PMID:8145243<ref>PMID:8145243</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1glp" 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]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Glutathione transferase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Coll, M]]	+	[[Category: Coll M]]
-	[[Category: Garcia-Saez, I]]	+	[[Category: Garcia-Saez I]]

OCA at 11:25, 28 July 2021

OCA — Wed, 28 Jul 2021 11:25:34 GMT

←Older revision		Revision as of 11:25, 28 July 2021
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	<StructureSection load='1glp' size='340' side='right'caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1glp' size='340' side='right'caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1GLP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GLP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></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>
-	<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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [~~http~~://pdbe.org/1glp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1glp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1glp 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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [https://pdbe.org/1glp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [https://www.ebi.ac.uk/pdbsum/1glp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1glp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GSTP1_MOUSE GSTP1_MOUSE]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity).	+	[[https://www.uniprot.org/uniprot/GSTP1_MOUSE GSTP1_MOUSE]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:19, 23 October 2019

OCA — Wed, 23 Oct 2019 09:19:14 GMT

←Older revision		Revision as of 09:19, 23 October 2019
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	==1.8 ANGSTROMS MOLECULAR STRUCTURE OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS==		==1.8 ANGSTROMS MOLECULAR STRUCTURE OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS==
-	<StructureSection load='1glp' size='340' side='right' caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1glp' size='340' side='right'caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLP FirstGlance]. <br>
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/1glp_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/1glp_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
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	</div>		</div>
	<div class="pdbe-citations 1glp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1glp" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Coll, M]]		[[Category: Coll, M]]
	[[Category: Garcia-Saez, I]]		[[Category: Garcia-Saez, I]]

OCA at 06:35, 29 November 2017

OCA — Wed, 29 Nov 2017 06:35:45 GMT

←Older revision		Revision as of 06:35, 29 November 2017
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		+
	==1.8 ANGSTROMS MOLECULAR STRUCTURE OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS==		==1.8 ANGSTROMS MOLECULAR STRUCTURE OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS==
	<StructureSection load='1glp' size='340' side='right' caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1glp' size='340' side='right' caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [http://pdbe.org/1glp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [http://www.ebi.ac.uk/pdbsum/1glp 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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [http://pdbe.org/1glp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [http://www.ebi.ac.uk/pdbsum/1glp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1glp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 1glp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1glp" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Glutathione S-transferase\|Glutathione S-transferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:43, 9 February 2016

OCA — Tue, 09 Feb 2016 03:43:48 GMT

←Older revision		Revision as of 03:43, 9 February 2016
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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=1glp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 18:17, 10 September 2015

OCA — Thu, 10 Sep 2015 18:17:32 GMT

←Older revision		Revision as of 18:17, 10 September 2015
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	<StructureSection load='1glp' size='340' side='right' caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1glp' size='340' side='right' caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [http://www.ebi.ac.uk/pdbsum/1glp 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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [http://pdbe.org/1glp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [http://www.ebi.ac.uk/pdbsum/1glp PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1glp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Coll, M]]		[[Category: Coll, M]]
	[[Category: Garcia-Saez, I]]		[[Category: Garcia-Saez, I]]

OCA at 04:11, 25 December 2014

OCA — Thu, 25 Dec 2014 04:11:01 GMT

←Older revision		Revision as of 04:11, 25 December 2014
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	<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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [http://www.ebi.ac.uk/pdbsum/1glp 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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [http://www.ebi.ac.uk/pdbsum/1glp PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GSTP1_MOUSE GSTP1_MOUSE]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 20:53, 22 December 2014

OCA — Mon, 22 Dec 2014 20:53:50 GMT

←Older revision		Revision as of 20:53, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLP FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [http://www.ebi.ac.uk/pdbsum/1glp 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=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [http://www.ebi.ac.uk/pdbsum/1glp PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 34:
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Coll, M.]]	+	[[Category: Coll, M]]
-	[[Category: Garcia-Saez, I.]]	+	[[Category: Garcia-Saez, I]]

OCA at 10:45, 28 September 2014

OCA — Sun, 28 Sep 2014 10:45:10 GMT

←Older revision		Revision as of 10:45, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1glp.~~png\|left~~\|200px]]	+	==1.8 ANGSTROMS MOLECULAR STRUCTURE OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS==
		+	<StructureSection load='1glp' size='340' side='right' caption='[[1glp]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1glp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLP FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1glp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1glp RCSB], [http://www.ebi.ac.uk/pdbsum/1glp PDBsum]</span></td></tr>
		+	<table>
		+	== 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/gl/1glp_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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The three-dimensional crystal structure of pi class glutathione S-transferase YfYf from mouse liver complexed with the inhibitor S-(p-nitrobenzyl)glutathione has been determined at 1.8 A resolution by X-ray diffraction. In addition two complexes with glutathione sulphonic acid and S-hexylglutathione have been determined at resolutions of 1.9 and 2.2 A, respectively. The high resolution of the S-(p-nitrobenzyl)glutathione complex allows a detailed analysis of the active site including the hydrophobic (H-) subsite. The nitrobenzyl moiety occupies a hydrophobic pocket with its aromatic ring sandwiched between Phe8 and the hydroxyl group of Tyr108. An insertion of two residues Gly41 and Leu42, with respect to the pig enzyme, splits helix alpha B into an alpha-helix and a 3(10) helix. Water bridges between carbonyl oxygen atoms of the alpha-helix at its C terminus and the amide NH groups of the 3(10) helix at its N terminus provide structural continuity between these two secondary elements. Tyr7 appears to be the only residue close to the sulphur atom of glutathione, while three conserved water molecules lie in the surrounding area in all complexes. The enzyme mechanism is discussed on the basis of the structural analysis.

-	~~{{STRUCTURE_1glp\| PDB=1glp \| SCENE= }}~~	+	Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors.,Garcia-Saez I, Parraga A, Phillips MF, Mantle TJ, Coll M J Mol Biol. 1994 Apr 1;237(3):298-314. PMID:8145243<ref>PMID:8145243</ref>

-	~~===1~~.~~8 ANGSTROMS MOLECULAR STRUCTURE OF MOUSE LIVER CLASS PI GLUTATHIONE~~ S~~-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_8145243}}~~	+	==See Also==
-		+	*[[Glutathione S-transferase\|Glutathione S-transferase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1glp~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLP OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:008145243<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Coll, M.]]		[[Category: Coll, M.]]
	[[Category: Garcia-Saez, I.]]		[[Category: Garcia-Saez, I.]]

OCA: Protected "1glp" [edit=sysop:move=sysop]

OCA — Wed, 21 Nov 2012 16:27:03 GMT

Protected "1glp" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:27, 21 November 2012