3nrr - Revision history

OCA at 09:19, 6 September 2023

OCA — Wed, 06 Sep 2023 09:19:55 GMT

←Older revision		Revision as of 09:19, 6 September 2023
Line 1:		Line 1:

	==Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP==		==Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP==
-	<StructureSection load='3nrr' size='340' side='right' caption='[[3nrr]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='3nrr' size='340' side='right'caption='[[3nrr]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3nrr]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Babbo Babbo~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3NRR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3nrr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Babesia_bovis Babesia bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NRR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=D16:TOMUDEX'>D16</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</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]] 1.8Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3i3r\|3i3r]], [[3k2h\|3k2h]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=D16:TOMUDEX'>D16</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBOV_II000780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5865 BABBO])</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=3nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nrr OCA], [https://pdbe.org/3nrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nrr RCSB], [https://www.ebi.ac.uk/pdbsum/3nrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nrr 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/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] </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=3nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nrr OCA], [~~http~~://pdbe.org/3nrr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3nrr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3nrr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3nrr ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/A7ASX7_BABBO A7ASX7_BABBO]] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389]	+	[https://www.uniprot.org/uniprot/A7ASX7_BABBO A7ASX7_BABBO] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389]
	== 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/nr/3nrr_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nr/3nrr_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 3nrr" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3nrr" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Dihydrofolate reductase 3D structures\|Dihydrofolate reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Babbo~~]]	+	[[Category: Babesia bovis]]
-	[[Category: ~~Thymidylate synthase]]~~	+	[[Category: Large Structures]]
-	~~[[Category: Structural genomic]]~~	+
-	~~[[Category: Babesiosis]]~~	+
-	~~[[Category: Dhfr]]~~	+
-	~~[[Category: Dihydrofolate reductase]]~~	+
-	~~[[Category: Dump]]~~	+
-	~~[[Category: Methyltransferase]]~~	+
-	~~[[Category: Nadp]]~~	+
-	~~[[Category: Niaid]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Raltitrexed]]~~	+
-	~~[[Category: Ssgcid]]~~	+
-	~~[[Category: Thya]]~~	+
-	~~[[Category: Tomudex]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: T~~]]	+

OCA at 08:35, 8 November 2017

OCA — Wed, 08 Nov 2017 08:35:06 GMT

←Older revision		Revision as of 08:35, 8 November 2017
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 3nrr" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3nrr" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Dihydrofolate reductase\|Dihydrofolate reductase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:29, 4 August 2016

OCA — Thu, 04 Aug 2016 19:29:00 GMT

←Older revision		Revision as of 19:29, 4 August 2016
Line 1:		Line 1:
		+
	==Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP==		==Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP==
	<StructureSection load='3nrr' size='340' side='right' caption='[[3nrr]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3nrr' size='340' side='right' caption='[[3nrr]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3nrr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Babesia_bovis Babesia bovis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NRR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3nrr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Babbo Babbo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NRR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=D16:TOMUDEX'>D16</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=D16:TOMUDEX'>D16</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3i3r\|3i3r]], [[3k2h\|3k2h]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3i3r\|3i3r]], [[3k2h\|3k2h]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBOV_II000780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5865 ~~Babesia bovis~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBOV_II000780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5865 BABBO])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] </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=3nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nrr RCSB], [http://www.ebi.ac.uk/pdbsum/3nrr 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=3nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nrr OCA], [http://pdbe.org/3nrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nrr RCSB], [http://www.ebi.ac.uk/pdbsum/3nrr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nrr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<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=3nrr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	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 3nrr" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Babesia bovis~~]]	+	[[Category: Babbo]]
	[[Category: Thymidylate synthase]]		[[Category: Thymidylate synthase]]
	[[Category: Structural genomic]]		[[Category: Structural genomic]]

OCA at 12:24, 25 December 2014

OCA — Thu, 25 Dec 2014 12:24:30 GMT

←Older revision		Revision as of 12:24, 25 December 2014
Line 9:		Line 9:
	<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=3nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nrr RCSB], [http://www.ebi.ac.uk/pdbsum/3nrr 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=3nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nrr RCSB], [http://www.ebi.ac.uk/pdbsum/3nrr PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/A7ASX7_BABBO A7ASX7_BABBO]] Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism (By similarity).[PIRNR:PIRNR000389]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:27, 9 December 2014

OCA — Tue, 09 Dec 2014 11:27:27 GMT

←Older revision		Revision as of 11:27, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3nrr.~~png~~\|~~left~~\|200px]]	+	==Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP==
		+	<StructureSection load='3nrr' size='340' side='right' caption='[[3nrr]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3nrr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Babesia_bovis Babesia bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NRR FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=D16:TOMUDEX'>D16</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3i3r\|3i3r]], [[3k2h\|3k2h]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BBOV_II000780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5865 Babesia bovis])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] </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=3nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nrr RCSB], [http://www.ebi.ac.uk/pdbsum/3nrr 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/nr/3nrr_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 ==
		+	Babesiosis is a tick-borne disease caused by eukaryotic Babesia parasites which are morphologically similar to Plasmodium falciparum, the causative agent of malaria in humans. Like Plasmodium, different species of Babesia are tuned to infect different mammalian hosts, including rats, dogs, horses and cattle. Most species of Plasmodium and Babesia possess an essential bifunctional enzyme for nucleotide synthesis and folate metabolism: dihydrofolate reductase-thymidylate synthase. Although thymidylate synthase is highly conserved across organisms, the bifunctional form of this enzyme is relatively uncommon in nature. The structural characterization of dihydrofolate reductase-thymidylate synthase in Babesia bovis, the causative agent of babesiosis in livestock cattle, is reported here. The apo state is compared with structures that contain dUMP, NADP and two different antifolate inhibitors: pemetrexed and raltitrexed. The complexes reveal modes of binding similar to that seen in drug-resistant malaria strains and point to the utility of applying structural studies with proven cancer chemotherapies towards infectious disease research.

-	~~{{STRUCTURE_3nrr\| PDB=3nrr \| SCENE= }}~~	+	Inhibitor-bound complexes of dihydrofolate reductase-thymidylate synthase from Babesia bovis.,Begley DW, Edwards TE, Raymond AC, Smith ER, Hartley RC, Abendroth J, Sankaran B, Lorimer DD, Myler PJ, Staker BL, Stewart LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1070-7. Epub 2011 Aug 16. PMID:21904052<ref>PMID:21904052</ref>

-	~~===Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP~~, ~~Raltitrexed and NADP===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_21904052}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3nrr]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Babesia_bovis Babesia bovis]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA].~~	+

	==See Also==		==See Also==
	*[[Dihydrofolate reductase\|Dihydrofolate reductase]]		*[[Dihydrofolate reductase\|Dihydrofolate reductase]]
-	*[[Thymidylate synthase\|Thymidylate synthase]]	+	== References ==
-		+	<references/>
-	==~~Reference~~==	+	__TOC__
-	<~~ref group="xtra">PMID:021904052<~~/~~ref~~><~~references group="xtra"~~/>	+	</StructureSection>
	[[Category: Babesia bovis]]		[[Category: Babesia bovis]]
	[[Category: Thymidylate synthase]]		[[Category: Thymidylate synthase]]
-	[[Category: ~~SSGCID, Seattle~~ Structural ~~Genomics Center for Infectious Disease.~~]]	+	[[Category: Structural genomic]]
	[[Category: Babesiosis]]		[[Category: Babesiosis]]
	[[Category: Dhfr]]		[[Category: Dhfr]]
Line 28:		Line 46:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Raltitrexed]]		[[Category: Raltitrexed]]
-	[[Category: Seattle structural genomics center for infectious disease]]
	[[Category: Ssgcid]]		[[Category: Ssgcid]]
-	[[Category: Structural genomic]]
	[[Category: Thya]]		[[Category: Thya]]
-	[[Category: Thymidylate synthase]]
	[[Category: Tomudex]]		[[Category: Tomudex]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: T]]		[[Category: T]]

OCA at 16:38, 20 October 2012

OCA — Sat, 20 Oct 2012 16:38:09 GMT

←Older revision		Revision as of 16:38, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3nrr]] is a 2 chain structure of [~~[Dihydrofolate reductase]] and [[Thymidylate synthase]~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA].	+	[[3nrr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Babesia_bovis Babesia bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA].

	==See Also==		==See Also==
Line 16:		Line 16:
	==Reference==		==Reference==
	<ref group="xtra">PMID:021904052</ref><references group="xtra"/>		<ref group="xtra">PMID:021904052</ref><references group="xtra"/>
		+	[[Category: Babesia bovis]]
	[[Category: Thymidylate synthase]]		[[Category: Thymidylate synthase]]
	[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]		[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]

OCA at 06:31, 10 October 2012

OCA — Wed, 10 Oct 2012 06:31:47 GMT

←Older revision		Revision as of 06:31, 10 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3nrr]] is a 2 chain structure of [[Dihydrofolate reductase]] and [[Thymidylate synthase]~~] with sequence from [http://en.wikipedia.org/wiki/Babesia_bovis Babesia bovis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA].	+	[[3nrr]] is a 2 chain structure of [[Dihydrofolate reductase]] and [[Thymidylate synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA].

	==See Also==		==See Also==
Line 16:		Line 16:
	==Reference==		==Reference==
	<ref group="xtra">PMID:021904052</ref><references group="xtra"/>		<ref group="xtra">PMID:021904052</ref><references group="xtra"/>
-	[[Category: Babesia bovis]]
	[[Category: Thymidylate synthase]]		[[Category: Thymidylate synthase]]
	[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]		[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]

OCA at 22:19, 26 July 2012

OCA — Thu, 26 Jul 2012 22:19:21 GMT

←Older revision		Revision as of 22:19, 26 July 2012
Line 1:		Line 1:
	[[Image:3nrr.png\|left\|200px]]		[[Image:3nrr.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3nrr", 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_3nrr\| PDB=3nrr \| SCENE= }}		{{STRUCTURE_3nrr\| PDB=3nrr \| SCENE= }}

	===Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP===		===Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_21904052}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 21904052 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_21904052}}		{{ABSTRACT_PUBMED_21904052}}

	==About this Structure==		==About this Structure==
-	[[3nrr]] is a 2 chain structure of [[Dihydrofolate reductase]] with sequence from [http://en.wikipedia.org/wiki/Babesia_bovis Babesia bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA].	+	[[3nrr]] is a 2 chain structure of [[Dihydrofolate reductase]] and [[Thymidylate synthase]] with sequence from [http://en.wikipedia.org/wiki/Babesia_bovis Babesia bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA].

	==See Also==		==See Also==
-	*[[Dihydrofolate reductase]]	+	*[[Dihydrofolate reductase\|Dihydrofolate reductase]]
		+	*[[Thymidylate synthase\|Thymidylate synthase]]

	==Reference==		==Reference==

OCA: Protected "3nrr" [edit=sysop:move=sysop]

OCA — Wed, 21 Sep 2011 05:14:01 GMT

Protected "3nrr" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:14, 21 September 2011

OCA at 05:13, 21 September 2011

OCA — Wed, 21 Sep 2011 05:13:59 GMT

←Older revision		Revision as of 05:13, 21 September 2011
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3nrr.png\|left\|200px]]
-	[[Image:3nrr.~~jpg~~\|left\|200px]]	+

	<!--		<!--
Line 12:		Line 11:
	===Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP===		===Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21904052}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21904052 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21904052}}

	==About this Structure==		==About this Structure==
-	~~3NRR~~ is a 2 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Babesia_bovis Babesia bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA].	+	[[3nrr]] is a 2 chain structure of [[Dihydrofolate reductase]] with sequence from [http://en.wikipedia.org/wiki/Babesia_bovis Babesia bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRR OCA].
		+
		+	==See Also==
		+	*[[Dihydrofolate reductase]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021904052</ref><references group="xtra"/>
	[[Category: Babesia bovis]]		[[Category: Babesia bovis]]
	[[Category: Thymidylate synthase]]		[[Category: Thymidylate synthase]]
Line 35:		Line 46:
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: T]]		[[Category: T]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 14 16:24:13 2010''