5fwg - Revision history

OCA at 06:51, 9 August 2023

OCA — Wed, 09 Aug 2023 06:51:31 GMT

←Older revision		Revision as of 06:51, 9 August 2023
Line 1:		Line 1:

	==TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE==		==TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE==
-	<StructureSection load='5fwg' size='340' side='right' caption='[[5fwg]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5fwg' size='340' side='right'caption='[[5fwg]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fwg]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5FWG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fwg]] is a 2 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=5FWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FWG FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=GPR:(9R,10R)~~-~~9-(S-GLUTATHIONYL)-10-HYDROXY-9~~,~~10-DIHYDROPHENANTHRENE'>GPR</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]] 2Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene>, <scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">CDNA INSERT OF 3~~-3 (M1-1) ~~ENZY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [https://pdbe.org/5fwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB], [https://www.ebi.ac.uk/pdbsum/5fwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fwg ProSAT]</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=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [~~http~~://pdbe.org/5fwg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5fwg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5fwg ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://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.	+	[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]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/5fwg_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/5fwg_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>
Line 31:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 5fwg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5fwg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Glutathione transferase~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Armstrong~~, R N~~]]	+	[[Category: Armstrong RN]]
-	[[Category: Gilliland~~, G L~~]]	+	[[Category: Gilliland GL]]
-	[[Category: Parsons~~, J F~~]]	+	[[Category: Parsons JF]]
-	[[Category: Xiao, G]]	+	[[Category: Xiao G]]
-	~~[[Category: 5-fluorotryptophan]]~~	+
-	~~[[Category: Three-dimensional structure]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Unnatural amino acid~~]]	+

OCA at 07:23, 29 November 2017

OCA — Wed, 29 Nov 2017 07:23:50 GMT

←Older revision		Revision as of 07:23, 29 November 2017
Line 1:		Line 1:
		+
	==TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE==		==TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE==
	<StructureSection load='5fwg' size='340' side='right' caption='[[5fwg]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5fwg' size='340' side='right' caption='[[5fwg]], [[Resolution\|resolution]] 2.00Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF 3-3 (M1-1) ENZY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF 3-3 (M1-1) ENZY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [http://pdbe.org/5fwg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB], [http://www.ebi.ac.uk/pdbsum/5fwg 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=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [http://pdbe.org/5fwg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB], [http://www.ebi.ac.uk/pdbsum/5fwg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fwg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 5fwg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5fwg" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Glutathione S-transferase\|Glutathione S-transferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:03, 8 February 2016

OCA — Mon, 08 Feb 2016 06:03:08 GMT

←Older revision		Revision as of 06:03, 8 February 2016
Line 2:		Line 2:
	<StructureSection load='5fwg' size='340' side='right' caption='[[5fwg]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5fwg' size='340' side='right' caption='[[5fwg]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fwg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FWG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fwg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FWG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF 3-3 (M1-1) ENZY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF 3-3 (M1-1) ENZY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB], [http://www.ebi.ac.uk/pdbsum/5fwg 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=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [http://pdbe.org/5fwg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB], [http://www.ebi.ac.uk/pdbsum/5fwg PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	<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=5fwg ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 29:
	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 5fwg" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
-	[[Category: Rattus norvegicus]]
	[[Category: Armstrong, R N]]		[[Category: Armstrong, R N]]
	[[Category: Gilliland, G L]]		[[Category: Gilliland, G L]]

OCA at 21:10, 24 December 2014

OCA — Wed, 24 Dec 2014 21:10:02 GMT

←Older revision		Revision as of 21:10, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5fwg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FWG FirstGlance]. <br>		<table><tr><td colspan='2'>[[5fwg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FWG FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF 3-3 (M1-1) ENZY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF 3-3 (M1-1) ENZY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB], [http://www.ebi.ac.uk/pdbsum/5fwg 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=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB], [http://www.ebi.ac.uk/pdbsum/5fwg PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://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]]
Line 36:		Line 38:
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Armstrong, R N.]]	+	[[Category: Armstrong, R N]]
-	[[Category: Gilliland, G L.]]	+	[[Category: Gilliland, G L]]
-	[[Category: Parsons, J F.]]	+	[[Category: Parsons, J F]]
-	[[Category: Xiao, G.]]	+	[[Category: Xiao, G]]
	[[Category: 5-fluorotryptophan]]		[[Category: 5-fluorotryptophan]]
-	[[Category: Glutathione transferase]]
	[[Category: Three-dimensional structure]]		[[Category: Three-dimensional structure]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Unnatural amino acid]]		[[Category: Unnatural amino acid]]

OCA: Protected "5fwg" [edit=sysop:move=sysop]

OCA — Thu, 05 Jun 2014 07:44:34 GMT

Protected "5fwg" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:44, 5 June 2014

OCA at 07:44, 5 June 2014

OCA — Thu, 05 Jun 2014 07:44:30 GMT

←Older revision		Revision as of 07:44, 5 June 2014
Line 1:		Line 1:
-	~~{{Seed}}~~	+	==TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE==
-	[[~~Image:~~5fwg.~~png~~\|~~left~~\|200px]]	+	<StructureSection load='5fwg' size='340' side='right' caption='[[5fwg]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5fwg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FWG FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPR:(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE'>GPR</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF 3-3 (M1-1) ENZY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB], [http://www.ebi.ac.uk/pdbsum/5fwg 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/fw/5fwg_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 catalytic characteristics and structure of the M1-1 isoenzyme of rat glutathione (GSH) transferase in which all four tryptophan residues in each monomer are replaced with 5-fluorotryptophan are described. The fluorine-for-hydrogen substitution does not change the interaction of the enzyme with GSH even though two tryptophan residues (Trp7 and Trp45) are involved in direct hydrogen-bonding interactions with the substrate. The rate constants for association and dissociation of the peptide, measured by stopped-flow spectrometry, remain unchanged by the unnatural amino acid. The 5-FTrp-substituted enzyme exhibits a kcat of 73 s-1 as compared to 18 s-1 for the native enzyme toward 1-chloro-2,4-dinitrobenzene. That the increase in the turnover number is due to an enhanced rate of product release in the mutant is confirmed by the kinetics of the approach to equilibrium for binding of the product. The crystal structure of the 5-FTrp-containing enzyme was solved at a resolution of 2.0 A by difference Fourier techniques. The structure reveals local conformational changes in the structural elements that define the approach to the active site which are attributed to steric interactions of the fluorine atoms associated with 5-FTrp146 and 5-FTrp214 in domain II. These changes appear to result in the enhanced rate of product release. This structure represents the first of a protein substituted with 5-fluorotryptophan.

-	<!--	+	Enzymes harboring unnatural amino acids: mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan.,Parsons JF, Xiao G, Gilliland GL, Armstrong RN Biochemistry. 1998 May 5;37(18):6286-94. PMID:9572843<ref>PMID:9572843</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_5fwg"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display~~.	+
-	-->	+
-	~~{{STRUCTURE_5fwg\| PDB=5fwg \| SCENE= }}~~	+

-	~~===TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	~~<!--~~	+	*[[Glutathione S-transferase\|Glutathione S-transferase]]
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_9572843}}, adds the Publication Abstract to the page~~	+	== References ==
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 9572843 is the PubMed ID number.~~	+	<references/>
-	~~-->~~	+	__TOC__
-	~~{{ABSTRACT_PUBMED_9572843}}~~	+	</StructureSection>
-		+
-	==~~About this Structure~~==	+
-	~~5FWG is a 2 chains structure of sequences from~~ [~~http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from~~ [~~http://oca.weizmann.ac.il/oca~~-~~bin/ocashort?id=5FWG OCA~~].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:9572843<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
Line 33:		Line 43:
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Three-dimensional structure]]		[[Category: Three-dimensional structure]]
		+	[[Category: Transferase]]
	[[Category: Unnatural amino acid]]		[[Category: Unnatural amino acid]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 19:39:38 2009''

OCA at 17:39, 16 February 2009

OCA — Mon, 16 Feb 2009 17:39:38 GMT

←Older revision		Revision as of 17:39, 16 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	5FWG is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA].	+	5FWG is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA].

	==Reference==		==Reference==
-	Enzymes harboring unnatural amino acids: mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan., Parsons JF, Xiao G, Gilliland GL, Armstrong RN, Biochemistry. 1998 May 5;37(18):6286-94. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/9572843 9572843]~~	+	<ref group="xtra">PMID:9572843</ref><references group="xtra"/>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Single protein]]
	[[Category: Armstrong, R N.]]		[[Category: Armstrong, R N.]]
	[[Category: Gilliland, G L.]]		[[Category: Gilliland, G L.]]
Line 36:		Line 35:
	[[Category: Unnatural amino acid]]		[[Category: Unnatural amino acid]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Sep 3 10~~:32:~~37 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 19:39:38 2009''

OCA at 07:32, 3 September 2008

OCA — Wed, 03 Sep 2008 07:32:38 GMT

←Older revision		Revision as of 07:32, 3 September 2008
Line 14:		Line 14:

	<!--		<!--
-	The line below this paragraph, {{~~ABSTRACT_PUBMED_8110735~~}}, adds the Publication Abstract to the page	+	The line below this paragraph, {{ABSTRACT_PUBMED_9572843}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where ~~8110735~~ is the PubMed ID number.	+	(as it appears on PubMed at http://www.pubmed.gov), where 9572843 is the PubMed ID number.
	-->		-->
-	{{~~ABSTRACT_PUBMED_8110735~~}}	+	{{ABSTRACT_PUBMED_9572843}}

	==About this Structure==		==About this Structure==
Line 23:		Line 23:

	==Reference==		==Reference==
-	~~Structure~~ and ~~function~~ of the ~~xenobiotic substrate binding site~~ of a glutathione S-transferase ~~as revealed by X~~-~~ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene~~., ~~Ji X~~, ~~Johnson WW~~, ~~Sesay MA, Dickert L, Prasad SM, Ammon HL~~, Armstrong RN~~, Gilliland GL~~, Biochemistry. ~~1994 Feb 8~~;33(5):~~1043~~-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/~~8110735 8110735~~]	+	Enzymes harboring unnatural amino acids: mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan., Parsons JF, Xiao G, Gilliland GL, Armstrong RN, Biochemistry. 1998 May 5;37(18):6286-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9572843 9572843]
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
Line 36:		Line 36:
	[[Category: Unnatural amino acid]]		[[Category: Unnatural amino acid]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Jul~~ 3 14:02:26 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 3 10:32:37 2008''

OCA at 11:02, 3 July 2008

OCA — Thu, 03 Jul 2008 11:02:26 GMT

←Older revision		Revision as of 11:02, 3 July 2008
Line 1:		Line 1:
-	[[Image:5fwg.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:5fwg.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_5fwg\| PDB=5fwg \| SCENE= }}		{{STRUCTURE_5fwg\| PDB=5fwg \| SCENE= }}

-	~~'''~~TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE~~'''~~	+	===TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE===


-	~~==Overview==~~	+	<!--
-	The ~~three-dimensional structures of isoenzyme 3-3 of glutathione (GSH) transferase complexed with (9R~~,~~10R)- and (9S~~,~~10S)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene [(9R,10R)-2 and (9S,10S)-2], which are~~ the ~~products of the addition of GSH~~ to ~~phenanthrene 9,10-oxide, have been determined at resolutions of 1.9 and 1.8 A, respectively. The structures indicate that~~ the ~~xenobiotic substrate binding site is a hydrophobic cavity defined by the side chains of Y6, W7, V9, and L12 from domain I~~ (~~the GSH binding domain) and I111, Y115, F208, and S209 in domain II of the protein~~. ~~All of these residues are located in variable-sequence regions of the primary structure of class mu isoenzymes~~. ~~Three of the eight residues (V9, I111, and S209~~) ~~of isoenzyme 3-3 that are in direct van der Waals contact with the dihydrophenanthrenyl portion of the products are mutated (V9I~~, ~~I111A, and S209A) in the related isoenzyme 4-4. These three residues are implicated in control of the stereoselectivity of the class mu isoenzymes. The hydroxyl group of Y115~~ is ~~found to be hydrogen-bonded to~~ the ~~10-hydroxyl group of (9S,10S)-2, a fact suggesting that this residue could act as an electrophile to stabilize the transition state for the addition of GSH to epoxides~~. ~~The Y115F mutant isoenzyme 3~~-~~3 is about 100~~-fold less efficient than the native enzyme in catalyzing the addition of GSH to phenanthrene 9,10-oxide and about 50-fold less efficient in the Michael addition of GSH to 4-phenyl-3-buten-2-one. The side chain of Y115 is positioned so as to act as a general-acid catalytic group for two types of reactions that would benefit from electrophilic assistance. The results are consistent with the notion that domain II, which harbors most of the variability in primary structure, plays a crucial role in defining the substrate specificity of class mu isoenzymes.	+	The line below this paragraph, {{ABSTRACT_PUBMED_8110735}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 8110735 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_8110735}}

	==About this Structure==		==About this Structure==
Line 31:		Line 35:
	[[Category: Three-dimensional structure]]		[[Category: Three-dimensional structure]]
	[[Category: Unnatural amino acid]]		[[Category: Unnatural amino acid]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ ~~4 22~~:34:15 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:02:26 2008''

OCA at 19:34, 4 May 2008

OCA — Sun, 04 May 2008 19:34:15 GMT

←Older revision		Revision as of 19:34, 4 May 2008
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	[[Image:5fwg.gif\|left\|200px]]		[[Image:5fwg.gif\|left\|200px]]

-	~~{{Structure~~	+	<!--
-	~~\|PDB= 5fwg \|SIZE=350\|CAPTION= <scene name='initialview01'>5fwg</scene>~~, ~~resolution 2~~.~~0Å~~	+	The line below this paragraph, containing "STRUCTURE_5fwg", creates the "Structure Box" on the page.
-	~~\|SITE= <scene name='pdbsite=GPS:Active+Site+Defined+Largely+By+These+Residues'>GPS</scene>~~	+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	~~\|LIGAND= <scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene>, <scene name='pdbligand=GPR:~~(~~9R,10R~~)~~-9-~~(~~S-GLUTATHIONYL~~)~~-10-HYDROXY-9~~,~~10-DIHYDROPHENANTHRENE'>GPR</scene>~~	+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	~~\|ACTIVITY= <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>~~	+	or leave the SCENE parameter empty for the default display.
-	~~\|GENE= CDNA INSERT OF 3~~-~~3 (M1~~-~~1) ENZY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])~~	+	-->
-	\|~~DOMAIN~~=	+	{{STRUCTURE_5fwg\| PDB=5fwg \| SCENE= }}
-	\|~~RELATEDENTRY~~=	+
-	\|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwg OCA], [http://www.ebi.ac.uk/pdbsum/5fwg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5fwg RCSB]</span>	+
-	}}	+

	'''TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE'''		'''TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE'''
Line 31:		Line 28:
	[[Category: Xiao, G.]]		[[Category: Xiao, G.]]
	[[Category: 5-fluorotryptophan]]		[[Category: 5-fluorotryptophan]]
-	[[Category: ~~glutathione~~ transferase]]	+	[[Category: Glutathione transferase]]
-	[[Category: ~~three~~-dimensional structure]]	+	[[Category: Three-dimensional structure]]
-	[[Category: ~~unnatural~~ amino acid]]	+	[[Category: Unnatural amino acid]]
-		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:34:15 2008''
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Mar 31 05~~:41:25 2008''	+