1e2g - Revision history

OCA at 08:45, 9 May 2024

OCA — Thu, 09 May 2024 08:45:52 GMT

←Older revision		Revision as of 08:45, 9 May 2024
Line 20:		Line 20:
	</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=1e2g 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=1e2g ConSurf].
	<div style="clear:both"></div>		<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.
		+
		+	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>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1e2g" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 09:57, 20 March 2024

OCA — Wed, 20 Mar 2024 09:57:46 GMT

←Older revision		Revision as of 09:57, 20 March 2024
Line 3:		Line 3:
	<StructureSection load='1e2g' size='340' side='right'caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='1e2g' size='340' side='right'caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1E2G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E2G 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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</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]] 1.7Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [https://pdbe.org/1e2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [https://www.ebi.ac.uk/pdbsum/1e2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2g 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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [~~http~~://pdbe.org/1e2g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1e2g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2g ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/KTHY_HUMAN KTHY_HUMAN]] Catalyzes the conversion of dTMP to dTDP.	+	[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]]
Line 21:		Line 20:
	</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=1e2g 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=1e2g ConSurf].
	<div style="clear:both"></div>		<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.
-
-	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>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1e2g" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__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: Transferase~~]]	+

OCA at 07:09, 9 December 2020

OCA — Wed, 09 Dec 2020 07:09:35 GMT

←Older revision		Revision as of 07:09, 9 December 2020
Line 1:		Line 1:

	==Human thymidylate kinase complexed with ADP, TDP and a magnesium-ion==		==Human thymidylate kinase complexed with ADP, TDP and a magnesium-ion==
-	<StructureSection load='1e2g' size='340' side='right' caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='1e2g' size='340' side='right'caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1E2G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1E2G 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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://pdbe.org/1e2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2g 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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://pdbe.org/1e2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 35:		Line 35:
	</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

OCA — Wed, 06 Mar 2019 07:39:48 GMT

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

	==Human thymidylate kinase complexed with ADP, TDP and a magnesium-ion==		==Human thymidylate kinase complexed with ADP, TDP and a magnesium-ion==
-	<StructureSection load='1e2g' size='340' side='right' caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='1e2g' size='340' side='right' caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e2g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2G 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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</td></tr>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e2/1e2g_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e2/1e2g_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 34:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Brundiers, R]]		[[Category: Brundiers, R]]

OCA at 09:53, 3 August 2017

OCA — Thu, 03 Aug 2017 09:53:00 GMT

←Older revision		Revision as of 09:53, 3 August 2017
Line 1:		Line 1:
-	==~~HUMAN THYMIDYLATE KINASE COMPLEXED WITH~~ ADP, TDP ~~AND A MAGNESIUM~~-~~ION~~==	+
		+	==Human thymidylate kinase complexed with ADP, TDP and a magnesium-ion==
	<StructureSection load='1e2g' size='340' side='right' caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='1e2g' size='340' side='right' caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e2g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2G 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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://pdbe.org/1e2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g 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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://pdbe.org/1e2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Brundiers, R]]		[[Category: Brundiers, R]]

OCA at 17:33, 8 February 2016

OCA — Mon, 08 Feb 2016 17:33:39 GMT

←Older revision		Revision as of 17:33, 8 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=1e2g ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 13:51, 10 September 2015

OCA — Thu, 10 Sep 2015 13:51:47 GMT

←Older revision		Revision as of 13:51, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1e2g' size='340' side='right' caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='1e2g' size='340' side='right' caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2G 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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g 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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://pdbe.org/1e2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1e2g" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Brundiers, R]]		[[Category: Brundiers, R]]

OCA at 01:00, 25 December 2014

OCA — Thu, 25 Dec 2014 01:00:49 GMT

←Older revision		Revision as of 01:00, 25 December 2014
Line 8:		Line 8:
	<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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g 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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://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]]

OCA at 22:25, 22 December 2014

OCA — Mon, 22 Dec 2014 22:25:24 GMT

←Older revision		Revision as of 22:25, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2G FirstGlance]. <br>		<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2G 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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g 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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g 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 32:		Line 32:
	[[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: Transferase]]		[[Category: Transferase]]

OCA at 10:54, 10 September 2014

OCA — Wed, 10 Sep 2014 10:54:22 GMT

←Older revision		Revision as of 10:54, 10 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1e2g.~~png~~\|~~left~~\|200px]]	+	==HUMAN THYMIDYLATE KINASE COMPLEXED WITH ADP, TDP AND A MAGNESIUM-ION==
		+	<StructureSection load='1e2g' size='340' side='right' caption='[[1e2g]], [[Resolution\|resolution]] 1.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1e2g]] 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=1E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E2G 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>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1nn3\|1nn3]], [[1e98\|1e98]], [[1e2e\|1e2e]], [[1e9e\|1e9e]], [[1e2q\|1e2q]], [[1nmx\|1nmx]], [[1e99\|1e99]], [[1nn5\|1nn5]], [[1nn1\|1nn1]], [[1nmz\|1nmz]], [[2xx3\|2xx3]], [[1e9d\|1e9d]], [[1e2f\|1e2f]], [[1nmy\|1nmy]], [[1e9f\|1e9f]], [[1nn0\|1nn0]], [[1e9c\|1e9c]]</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=1e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e2g RCSB], [http://www.ebi.ac.uk/pdbsum/1e2g 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/e2/1e2g_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_1e2g\| PDB=1e2g \| 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 ADP~~, ~~TDP AND A MAGNESIUM-ION===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_10873853}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1e2g]] 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=1E2G OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:010873853<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]