1rqr - Revision history

OCA at 08:26, 1 May 2024

OCA — Wed, 01 May 2024 08:26:23 GMT

←Older revision		Revision as of 08:26, 1 May 2024
Line 3:		Line 3:
	<StructureSection load='1rqr' size='340' side='right'caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>		<StructureSection load='1rqr' size='340' side='right'caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces~~ cattleya~~" kahan et al. 1979~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQR FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=5FD:5~~-~~FLUORO-5-DEOXYADENOSINE'>5FD</scene>~~, ~~<scene name='pdbligand=MET:METHIONINE'>MET</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]] 2.67Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~MSE~~:~~SELENOMETHIONINE~~'>~~MSE~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;~~'>~~[[1rqp\|1rqp]]~~</~~div~~><~~/td></tr>~~	+
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">fla ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</td></tr>~~	+
-	~~<tr id='activity~~'>~~<td class="sblockLbl"><b>Activity:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [https://pdbe.org/1rqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [https://www.ebi.ac.uk/pdbsum/1rqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqr 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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [https://pdbe.org/1rqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [https://www.ebi.ac.uk/pdbsum/1rqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqr ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/FLA_STRCT FLA_STRCT] Involved in the biosynthesis of fluorometabolites. Catalyzes the formation of a C-F bond by combining S-adenosyl-L-methionine (SAM) and fluoride to generate 5'-fluoro-5'-deoxyadenosine (5'-FDA) and L-methionine. It can also use 2'-deoxyadenosine in place of adenosine as substrate.<ref>PMID:12860396</ref> <ref>PMID:14765200</ref> <ref>PMID:16370017</ref> <ref>PMID:16604208</ref> <ref>PMID:16720268</ref> <ref>PMID:17985882</ref>
	== 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=1rqr 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=1rqr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Fluorine is the thirteenth most abundant element in the earth's crust, but fluoride concentrations in surface water are low and fluorinated metabolites are extremely rare. The fluoride ion is a potent nucleophile in its desolvated state, but is tightly hydrated in water and effectively inert. Low availability and a lack of chemical reactivity have largely excluded fluoride from biochemistry: in particular, fluorine's high redox potential precludes the haloperoxidase-type mechanism used in the metabolic incorporation of chloride and bromide ions. But fluorinated chemicals are growing in industrial importance, with applications in pharmaceuticals, agrochemicals and materials products. Reactive fluorination reagents requiring specialist process technologies are needed in industry and, although biological catalysts for these processes are highly sought after, only one enzyme that can convert fluoride to organic fluorine has been described. Streptomyces cattleya can form carbon-fluorine bonds and must therefore have evolved an enzyme able to overcome the chemical challenges of using aqueous fluoride. Here we report the sequence and three-dimensional structure of the first native fluorination enzyme, 5'-fluoro-5'-deoxyadenosine synthase, from this organism. Both substrate and products have been observed bound to the enzyme, enabling us to propose a nucleophilic substitution mechanism for this biological fluorination reaction.
-
-	Crystal structure and mechanism of a bacterial fluorinating enzyme.,Dong C, Huang F, Deng H, Schaffrath C, Spencer JB, O'Hagan D, Naismith JH Nature. 2004 Feb 5;427(6974):561-5. PMID:14765200<ref>PMID:14765200</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1rqr" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Streptomyces cattleya kahan et al. 1979]]
-	[[Category: Adenosyl-fluoride synthase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Deng, H~~]]	+	[[Category: Streptomyces cattleya]]
-	[[Category: ~~Dong, C~~]]	+	[[Category: Deng H]]
-	[[Category: ~~Hagan, D O~~]]	+	[[Category: Dong C]]
-	[[Category: Huang, F]]	+	[[Category: Huang F]]
-	[[Category: Naismith~~, J H~~]]	+	[[Category: Naismith JH]]
-	[[Category: ~~Schaffrath, C~~]]	+	[[Category: O'Hagan D]]
-	[[Category: ~~Spencer, J B~~]]	+	[[Category: Schaffrath C]]
-	[[Category: ~~Anti-parallel beta sheet]]~~	+	[[Category: Spencer JB]]
-	~~[[Category: Central 7 stranded beta sheet]]~~	+
-	~~[[Category: Fluorinase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 05:13, 15 June 2022

OCA — Wed, 15 Jun 2022 05:13:37 GMT

←Older revision		Revision as of 05:13, 15 June 2022
Line 3:		Line 3:
	<StructureSection load='1rqr' size='340' side='right'caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>		<StructureSection load='1rqr' size='340' side='right'caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1RQR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rqp\|1rqp]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rqp\|1rqp]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [~~http~~://pdbe.org/1rqr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1rqr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqr 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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [https://pdbe.org/1rqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [https://www.ebi.ac.uk/pdbsum/1rqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqr ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 13:32, 16 December 2020

OCA — Wed, 16 Dec 2020 13:32:10 GMT

OCA at 18:40, 24 January 2018

OCA — Wed, 24 Jan 2018 18:40:34 GMT

←Older revision		Revision as of 18:40, 24 January 2018
Line 1:		Line 1:
		+
	==Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex==		==Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex==
	<StructureSection load='1rqr' size='340' side='right' caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>		<StructureSection load='1rqr' size='340' side='right' caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>
Line 8:		Line 9:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [http://pdbe.org/1rqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [http://www.ebi.ac.uk/pdbsum/1rqr 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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [http://pdbe.org/1rqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [http://www.ebi.ac.uk/pdbsum/1rqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqr ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rq/1rqr_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rq/1rqr_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>

OCA at 21:48, 9 February 2016

OCA — Tue, 09 Feb 2016 21:48:02 GMT

←Older revision		Revision as of 21:48, 9 February 2016
Line 18:		Line 18:
	<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=1rqr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 02:20, 11 September 2015

OCA — Fri, 11 Sep 2015 02:20:43 GMT

←Older revision		Revision as of 02:20, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1rqr' size='340' side='right' caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>		<StructureSection load='1rqr' size='340' side='right' caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Streptomyces_cattleya Streptomyces~~ cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RQR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RQR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 Streptomyces cattleya])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [http://www.ebi.ac.uk/pdbsum/1rqr 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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [http://pdbe.org/1rqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [http://www.ebi.ac.uk/pdbsum/1rqr PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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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 1rqr" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Streptomyces cattleya kahan et al. 1979]]
	[[Category: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
-	[[Category: Streptomyces cattleya]]
	[[Category: Deng, H]]		[[Category: Deng, H]]
	[[Category: Dong, C]]		[[Category: Dong, C]]

OCA at 07:46, 6 January 2015

OCA — Tue, 06 Jan 2015 07:46:14 GMT

←Older revision		Revision as of 07:46, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RQR FirstGlance]. <br>		<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RQR FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 Streptomyces cattleya])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 Streptomyces cattleya])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [http://www.ebi.ac.uk/pdbsum/1rqr 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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [http://www.ebi.ac.uk/pdbsum/1rqr 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: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
	[[Category: Streptomyces cattleya]]		[[Category: Streptomyces cattleya]]
-	[[Category: Deng, H.]]	+	[[Category: Deng, H]]
-	[[Category: Dong, C.]]	+	[[Category: Dong, C]]
-	[[Category: Hagan, D O.]]	+	[[Category: Hagan, D O]]
-	[[Category: Huang, F.]]	+	[[Category: Huang, F]]
-	[[Category: Naismith, J H.]]	+	[[Category: Naismith, J H]]
-	[[Category: Schaffrath, C.]]	+	[[Category: Schaffrath, C]]
-	[[Category: Spencer, J B.]]	+	[[Category: Spencer, J B]]
	[[Category: Anti-parallel beta sheet]]		[[Category: Anti-parallel beta sheet]]
	[[Category: Central 7 stranded beta sheet]]		[[Category: Central 7 stranded beta sheet]]
	[[Category: Fluorinase]]		[[Category: Fluorinase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 16:21, 29 September 2014

OCA — Mon, 29 Sep 2014 16:21:09 GMT

←Older revision		Revision as of 16:21, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1rqr.~~png~~\|~~left~~\|200px]]	+	==Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex==
		+	<StructureSection load='1rqr' size='340' side='right' caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RQR FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 Streptomyces cattleya])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [http://www.ebi.ac.uk/pdbsum/1rqr 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/rq/1rqr_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 ==
		+	Fluorine is the thirteenth most abundant element in the earth's crust, but fluoride concentrations in surface water are low and fluorinated metabolites are extremely rare. The fluoride ion is a potent nucleophile in its desolvated state, but is tightly hydrated in water and effectively inert. Low availability and a lack of chemical reactivity have largely excluded fluoride from biochemistry: in particular, fluorine's high redox potential precludes the haloperoxidase-type mechanism used in the metabolic incorporation of chloride and bromide ions. But fluorinated chemicals are growing in industrial importance, with applications in pharmaceuticals, agrochemicals and materials products. Reactive fluorination reagents requiring specialist process technologies are needed in industry and, although biological catalysts for these processes are highly sought after, only one enzyme that can convert fluoride to organic fluorine has been described. Streptomyces cattleya can form carbon-fluorine bonds and must therefore have evolved an enzyme able to overcome the chemical challenges of using aqueous fluoride. Here we report the sequence and three-dimensional structure of the first native fluorination enzyme, 5'-fluoro-5'-deoxyadenosine synthase, from this organism. Both substrate and products have been observed bound to the enzyme, enabling us to propose a nucleophilic substitution mechanism for this biological fluorination reaction.

-	~~{{STRUCTURE_1rqr\| PDB=1rqr \| SCENE= }}~~	+	Crystal structure and mechanism of a bacterial fluorinating enzyme.,Dong C, Huang F, Deng H, Schaffrath C, Spencer JB, O'Hagan D, Naismith JH Nature. 2004 Feb 5;427(6974):561-5. PMID:14765200<ref>PMID:14765200</ref>

-	~~===Crystal structure and mechanism of a bacterial fluorinating enzyme~~, ~~product complex===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14765200}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1rqr]] is~~ a ~~3 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Streptomyces_cattleya Streptomyces cattleya]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:014765200<~~/~~ref~~><~~ref group="xtra">PMID:018774824</ref><references group="xtra"~~/>	+
	[[Category: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
	[[Category: Streptomyces cattleya]]		[[Category: Streptomyces cattleya]]

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

OCA — Fri, 04 Jan 2013 10:07:04 GMT

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

←Older revision

Revision as of 10:07, 4 January 2013

OCA at 10:07, 4 January 2013

OCA — Fri, 04 Jan 2013 10:07:02 GMT

←Older revision		Revision as of 10:07, 4 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1rqr.png\|left\|200px]]		[[Image:1rqr.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1rqr", 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_1rqr\| PDB=1rqr \| SCENE= }}		{{STRUCTURE_1rqr\| PDB=1rqr \| SCENE= }}

	===Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex===		===Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_14765200}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 14765200 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_14765200}}		{{ABSTRACT_PUBMED_14765200}}

	==About this Structure==		==About this Structure==
-	~~1RQR~~ is a 3 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA].	+	[[1rqr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~14765200~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:014765200</ref><ref group="xtra">PMID:018774824</ref><references group="xtra"/>
	[[Category: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
	[[Category: Streptomyces cattleya]]		[[Category: Streptomyces cattleya]]
Line 36:		Line 24:
	[[Category: Central 7 stranded beta sheet]]		[[Category: Central 7 stranded beta sheet]]
	[[Category: Fluorinase]]		[[Category: Fluorinase]]
-		+	[[Category: Transferase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 13:00:01 2009''~~	+

←Older revision		Revision as of 13:32, 16 December 2020
Line 1:		Line 1:

	==Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex==		==Crystal structure and mechanism of a bacterial fluorinating enzyme, product complex==
-	<StructureSection load='1rqr' size='340' side='right' caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>	+	<StructureSection load='1rqr' size='340' side='right'caption='[[1rqr]], [[Resolution\|resolution]] 2.67Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1RQR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1rqr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RQR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5FD:5-FLUORO-5-DEOXYADENOSINE'>5FD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rqp\|1rqp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rqp\|1rqp]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fla ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [http://pdbe.org/1rqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [http://www.ebi.ac.uk/pdbsum/1rqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqr ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqr OCA], [http://pdbe.org/1rqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rqr RCSB], [http://www.ebi.ac.uk/pdbsum/1rqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqr ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 36:		Line 36:
	[[Category: Streptomyces cattleya kahan et al. 1979]]		[[Category: Streptomyces cattleya kahan et al. 1979]]
	[[Category: Adenosyl-fluoride synthase]]		[[Category: Adenosyl-fluoride synthase]]
		+	[[Category: Large Structures]]
	[[Category: Deng, H]]		[[Category: Deng, H]]
	[[Category: Dong, C]]		[[Category: Dong, C]]