1e2d - Revision history

OCA at 08:10, 6 December 2023

2023-12-06T08:10:35Z

←Older revision		Revision as of 08:10, 6 December 2023
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	<StructureSection load='1e2d' size='340' side='right'caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='1e2d' size='340' side='right'caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1E2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E2D FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ADP:ADENOSINE~~-~~5-DIPHOSPHATE'>ADP</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</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]] 1.65Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9]~~ </~~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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [https://pdbe.org/1e2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [https://www.ebi.ac.uk/pdbsum/1e2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2d 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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [~~http~~://pdbe.org/1e2d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1e2d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2d ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/KTHY_HUMAN KTHY_HUMAN] Catalyzes the conversion of dTMP to dTDP.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: DTMP kinase]]~~	+	[[Category: Brundiers R]]
-	[[Category: Brundiers, R]]	+	[[Category: Goody RS]]
-	[[Category: Goody~~, R S~~]]	+	[[Category: Konrad M]]
-	[[Category: Konrad, M]]	+	[[Category: Lavie A]]
-	[[Category: Lavie, A]]	+	[[Category: Ostermann N]]
-	[[Category: Ostermann, N]]	+	[[Category: Reinstein J]]
-	[[Category: Reinstein, J]]	+	[[Category: Schlichting I]]
-	[[Category: Schlichting, I]]	+	[[Category: Veit T]]
-	[[Category: Veit, T]]	+
-	~~[[Category: P-loop]]~~	+
-	~~[[Category: Phosphotransferase]]~~	+
-	~~[[Category: Thymidylate kinase~~]]	+

OCA at 07:09, 9 December 2020

2020-12-09T07:09:27Z

←Older revision		Revision as of 07:09, 9 December 2020
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	==Human thymidylate kinase complexed with thymidine monophosphate, adenosine diphosphate and a magnesium-ion==		==Human thymidylate kinase complexed with thymidine monophosphate, adenosine diphosphate and a magnesium-ion==
-	<StructureSection load='1e2d' size='340' side='right' caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>	+	<StructureSection load='1e2d' size='340' side='right'caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1E2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1E2D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [http://pdbe.org/1e2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [http://www.ebi.ac.uk/pdbsum/1e2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2d 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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [http://pdbe.org/1e2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [http://www.ebi.ac.uk/pdbsum/1e2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2d ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	==See Also==		==See Also==
-	*[[Thymidylate kinase\|Thymidylate kinase]]	+	*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]
-	*[[Thymidylate synthase\|Thymidylate synthase]]	+	*[[Thymidylate synthase 3D structures\|Thymidylate synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Brundiers, R]]		[[Category: Brundiers, R]]

OCA at 07:39, 6 March 2019

2019-03-06T07:39:36Z

←Older revision		Revision as of 07:39, 6 March 2019
Line 1:		Line 1:

	==Human thymidylate kinase complexed with thymidine monophosphate, adenosine diphosphate and a magnesium-ion==		==Human thymidylate kinase complexed with thymidine monophosphate, adenosine diphosphate and a magnesium-ion==
-	<StructureSection load='1e2d' size='340' side='right' caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>	+	<StructureSection load='1e2d' size='340' side='right' caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2D FirstGlance]. <br>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1e2d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1e2d" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thymidylate kinase\|Thymidylate kinase]]
		+	*[[Thymidylate synthase\|Thymidylate synthase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:54, 13 December 2017

2017-12-13T07:54:11Z

←Older revision		Revision as of 07:54, 13 December 2017
Line 1:		Line 1:
-	==~~HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE~~, ~~ADENOSINE DIPHOSPHATE AND A MAGNESIUM~~-~~ION~~==	+
		+	==Human thymidylate kinase complexed with thymidine monophosphate, adenosine diphosphate and a magnesium-ion==
	<StructureSection load='1e2d' size='340' side='right' caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='1e2d' size='340' side='right' caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [http://pdbe.org/1e2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [http://www.ebi.ac.uk/pdbsum/1e2d 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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [http://pdbe.org/1e2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [http://www.ebi.ac.uk/pdbsum/1e2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2d ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e2/1e2d_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e2/1e2d_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 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1e2d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1e2d" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Thymidylate kinase\|Thymidylate kinase]]
-	*[[Thymidylate synthase\|Thymidylate synthase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:33, 9 February 2016

2016-02-09T15:33:07Z

←Older revision		Revision as of 15:33, 9 February 2016
Line 16:		Line 16:
	<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=1e2d ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 23:37, 10 September 2015

2015-09-10T23:37:15Z

←Older revision		Revision as of 23:37, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1e2d' size='340' side='right' caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='1e2d' size='340' side='right' caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2D FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [http://www.ebi.ac.uk/pdbsum/1e2d 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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [http://pdbe.org/1e2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [http://www.ebi.ac.uk/pdbsum/1e2d PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 26:		Line 26:
	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 1e2d" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Brundiers, R]]		[[Category: Brundiers, R]]

OCA at 19:45, 22 December 2014

2014-12-22T19:45:38Z

←Older revision		Revision as of 19:45, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2D FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [http://www.ebi.ac.uk/pdbsum/1e2d 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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [http://www.ebi.ac.uk/pdbsum/1e2d 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 36:		Line 36:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
-	[[Category: Brundiers, R.]]	+	[[Category: Brundiers, R]]
-	[[Category: Goody, R S.]]	+	[[Category: Goody, R S]]
-	[[Category: Konrad, M.]]	+	[[Category: Konrad, M]]
-	[[Category: Lavie, A.]]	+	[[Category: Lavie, A]]
-	[[Category: Ostermann, N.]]	+	[[Category: Ostermann, N]]
-	[[Category: Reinstein, J.]]	+	[[Category: Reinstein, J]]
-	[[Category: Schlichting, I.]]	+	[[Category: Schlichting, I]]
-	[[Category: Veit, T.]]	+	[[Category: Veit, T]]
	[[Category: P-loop]]		[[Category: P-loop]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]
	[[Category: Thymidylate kinase]]		[[Category: Thymidylate kinase]]

OCA at 10:44, 10 September 2014

2014-09-10T10:44:42Z

←Older revision		Revision as of 10:44, 10 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1e2d.~~png~~\|~~left~~\|200px]]	+	==HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE, ADENOSINE DIPHOSPHATE AND A MAGNESIUM-ION==
		+	<StructureSection load='1e2d' size='340' side='right' caption='[[1e2d]], [[Resolution\|resolution]] 1.65Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2D FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tmk\|3tmk]], [[2tmk\|2tmk]], [[1tmk\|1tmk]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2q\|1e2q]], [[1e2g\|1e2g]], [[1e98\|1e98]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=1e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2d RCSB], [http://www.ebi.ac.uk/pdbsum/1e2d 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/e2/1e2d_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 ==
		+	BACKGROUND: Thymidylate kinase (TMPK) is a nucleoside monophosphate kinase that catalyzes the reversible phosphoryltransfer between ATP and TMP to yield ADP and TDP. In addition to its vital role in supplying precursors for DNA synthesis, human TMPK has an important medical role participating in the activation of a number of anti-HIV prodrugs. RESULTS: Crystal structures of human TMPK in complex with TMP and ADP, TMP and the ATP analog AppNHp, TMP with ADP and the phosphoryl analog AlF(3), TDP and ADP, and the bisubstrate analog TP(5)A were determined. The conformations of the P-loop, the LID region, and the adenine-binding loop vary according to the nature of the complex. Substitution of ADP by AppNHp results in partial closure of the P-loop and the rotation of the TMP phosphate group to a catalytically unfavorable position, which rotates back in the AlF(3) complex to a position suitable for in-line attack. In the fully closed state observed in the TP(5)A and the TDP-ADP complexes, Asp15 interacts strongly with the 3'-hydroxyl group of TMP. CONCLUSIONS: The observed changes of nucleotide state and conformation and the corresponding protein structural changes are correlated with intermediates occurring along the reaction coordinate and show the sequence of events occurring during phosphate transfer. The low catalytic activity of human TMPK appears to be determined by structural changes required to achieve catalytic competence and it is suggested that a mechanism might exist to accelerate the activity.

-	~~{{STRUCTURE_1e2d\| PDB=1e2d \| SCENE= }}~~	+	Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate.,Ostermann N, Schlichting I, Brundiers R, Konrad M, Reinstein J, Veit T, Goody RS, Lavie A Structure. 2000 Jun 15;8(6):629-42. PMID:10873853<ref>PMID:10873853</ref>

-	~~===HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE~~, ~~ADENOSINE DIPHOSPHATE AND A MAGNESIUM-ION===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_10873853}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1e2d]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA].~~	+

	==See Also==		==See Also==
		+	*[[Thymidylate kinase\|Thymidylate kinase]]
	*[[Thymidylate synthase\|Thymidylate synthase]]		*[[Thymidylate synthase\|Thymidylate synthase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:010873853<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]

OCA at 14:19, 20 October 2012

2012-10-20T14:19:08Z

←Older revision		Revision as of 14:19, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1e2d]] is a 1 chain structure ~~of [[Thymidylate synthase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA].	+	[[1e2d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2D OCA].

	==See Also==		==See Also==

OCA: Protected "1e2d" [edit=sysop:move=sysop]

2012-07-26T14:46:14Z

Protected "1e2d" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:46, 26 July 2012