1e98 - Revision history

OCA at 08:48, 9 May 2024

OCA — Thu, 09 May 2024 08:48:04 GMT

←Older revision		Revision as of 08:48, 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=1e98 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=1e98 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The 60-fold reduced phosphorylation rate of azidothymidine (AZT) monophosphate (AZTMP), the partially activated AZT metabolite, by human thymidylate kinase (TMPK) severely limits the efficacy of this anti-HIV prodrug. Crystal structures of different TMPK nucleotide complexes indicate that steric hindrance by the azido group of AZTMP prevents formation of the catalytically active closed conformation of the P-loop of TMPK. The F105Y mutant and a chimeric mutant that contains sequences of the human and Escherichia coli enzyme phosphorylate AZTMP 20-fold faster than the wild-type enzyme. The structural basis of the increased activity is assigned to stabilization of the closed P-loop conformation.
		+
		+	Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP.,Ostermann N, Lavie A, Padiyar S, Brundiers R, Veit T, Reinstein J, Goody RS, Konrad M, Schlichting I J Mol Biol. 2000 Nov 17;304(1):43-53. PMID:11071809<ref>PMID:11071809</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1e98" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]		*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 09:59, 20 March 2024

OCA — Wed, 20 Mar 2024 09:59:57 GMT

←Older revision		Revision as of 09:59, 20 March 2024
Line 3:		Line 3:
	<StructureSection load='1e98' size='340' side='right'caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1e98' size='340' side='right'caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1E98 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E98 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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.9Å</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]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [https://pdbe.org/1e98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [https://www.ebi.ac.uk/pdbsum/1e98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e98 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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [~~http~~://pdbe.org/1e98 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1e98 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1e98 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=1e98 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=1e98 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The 60-fold reduced phosphorylation rate of azidothymidine (AZT) monophosphate (AZTMP), the partially activated AZT metabolite, by human thymidylate kinase (TMPK) severely limits the efficacy of this anti-HIV prodrug. Crystal structures of different TMPK nucleotide complexes indicate that steric hindrance by the azido group of AZTMP prevents formation of the catalytically active closed conformation of the P-loop of TMPK. The F105Y mutant and a chimeric mutant that contains sequences of the human and Escherichia coli enzyme phosphorylate AZTMP 20-fold faster than the wild-type enzyme. The structural basis of the increased activity is assigned to stabilization of the closed P-loop conformation.
-
-	Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP.,Ostermann N, Lavie A, Padiyar S, Brundiers R, Veit T, Reinstein J, Goody RS, Konrad M, Schlichting I J Mol Biol. 2000 Nov 17;304(1):43-53. PMID:11071809<ref>PMID:11071809</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1e98" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]		*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]
-	== 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: Padiyar S]]
-	[[Category: Padiyar, S]]	+	[[Category: Reintein J]]
-	[[Category: Reintein, J]]	+	[[Category: Schlichting I]]
-	[[Category: Schlichting, I]]	+	[[Category: Veit T]]
-	[[Category: Veit, T]]	+
-	~~[[Category: P-loop]]~~	+
-	~~[[Category: Phosphotransferase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 07:09, 9 December 2020

OCA — Wed, 09 Dec 2020 07:09:41 GMT

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

	==Wild type human thymidylate kinase complexed with AZTMP and ADP==		==Wild type human thymidylate kinase complexed with AZTMP and ADP==
-	<StructureSection load='1e98' size='340' side='right' caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1e98' size='340' side='right'caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1E98 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1E98 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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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;'>[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://pdbe.org/1e98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e98 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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://pdbe.org/1e98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e98 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Thymidylate kinase\|Thymidylate kinase]]	+	*[[Thymidylate kinase 3D structures\|Thymidylate kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Brundiers, R]]		[[Category: Brundiers, R]]

OCA at 07:40, 6 March 2019

OCA — Wed, 06 Mar 2019 07:40:02 GMT

←Older revision		Revision as of 07:40, 6 March 2019
Line 1:		Line 1:

	==Wild type human thymidylate kinase complexed with AZTMP and ADP==		==Wild type human thymidylate kinase complexed with AZTMP and ADP==
-	<StructureSection load='1e98' size='340' side='right' caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1e98' size='340' side='right' caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e98]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E98 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E98 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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[1e99\|1e99]], [[1e9a\|1e9a]], [[1e9b\|1e9b]], [[1e9c\|1e9c]], [[1e9d\|1e9d]], [[1e9e\|1e9e]], [[1e9f\|1e9f]]</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/e9/1e98_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e9/1e98_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 37:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Brundiers, R]]		[[Category: Brundiers, R]]

OCA at 03:50, 6 September 2017

OCA — Wed, 06 Sep 2017 03:50:15 GMT

←Older revision		Revision as of 03:50, 6 September 2017
Line 1:		Line 1:
		+
	==Wild type human thymidylate kinase complexed with AZTMP and ADP==		==Wild type human thymidylate kinase complexed with AZTMP and ADP==
	<StructureSection load='1e98' size='340' side='right' caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1e98' size='340' side='right' caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E98 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e98]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E98 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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://pdbe.org/1e98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://pdbe.org/1e98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e98 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e98 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Brundiers, R]]		[[Category: Brundiers, R]]

OCA at 17:21, 11 September 2015

OCA — Fri, 11 Sep 2015 17:21:43 GMT

←Older revision		Revision as of 17:21, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1e98' size='340' side='right' caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1e98' size='340' side='right' caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E98 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E98 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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://pdbe.org/1e98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 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 1e98" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
	[[Category: Brundiers, R]]		[[Category: Brundiers, R]]

OCA at 19:33, 25 December 2014

OCA — Thu, 25 Dec 2014 19:33:39 GMT

←Older revision		Revision as of 19:33, 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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 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 19:15, 22 December 2014

OCA — Mon, 22 Dec 2014 19:15:56 GMT

←Older revision		Revision as of 19:15, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E98 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E98 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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 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 35:		Line 35:
	[[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: Padiyar, S.]]	+	[[Category: Padiyar, S]]
-	[[Category: Reintein, J.]]	+	[[Category: Reintein, J]]
-	[[Category: Schlichting, I.]]	+	[[Category: Schlichting, I]]
-	[[Category: Veit, T.]]	+	[[Category: Veit, T]]
	[[Category: P-loop]]		[[Category: P-loop]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 04:06, 3 October 2014

OCA — Fri, 03 Oct 2014 04:06:04 GMT

←Older revision		Revision as of 04:06, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1e98\| PDB=1e98 \| SCENE= }}~~	+	==Wild type human thymidylate kinase complexed with AZTMP and ADP==
-	===Wild type human thymidylate kinase complexed with AZTMP and ADP===	+	<StructureSection load='1e98' size='340' side='right' caption='[[1e98]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~{{ABSTRACT_PUBMED_11071809}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1e98]] 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=1E98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E98 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=ATM:3-AZIDO-3-DEOXYTHYMIDINE-5-MONOPHOSPHATE'>ATM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e2d\|1e2d]], [[1e2e\|1e2e]], [[1e2f\|1e2f]], [[1e2g\|1e2g]], [[1e2q\|1e2q]], [[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=1e98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e98 RCSB], [http://www.ebi.ac.uk/pdbsum/1e98 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/e9/1e98_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The 60-fold reduced phosphorylation rate of azidothymidine (AZT) monophosphate (AZTMP), the partially activated AZT metabolite, by human thymidylate kinase (TMPK) severely limits the efficacy of this anti-HIV prodrug. Crystal structures of different TMPK nucleotide complexes indicate that steric hindrance by the azido group of AZTMP prevents formation of the catalytically active closed conformation of the P-loop of TMPK. The F105Y mutant and a chimeric mutant that contains sequences of the human and Escherichia coli enzyme phosphorylate AZTMP 20-fold faster than the wild-type enzyme. The structural basis of the increased activity is assigned to stabilization of the closed P-loop conformation.

-	~~==Function==~~	+	Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP.,Ostermann N, Lavie A, Padiyar S, Brundiers R, Veit T, Reinstein J, Goody RS, Konrad M, Schlichting I J Mol Biol. 2000 Nov 17;304(1):43-53. PMID:11071809<ref>PMID:11071809</ref>
-	~~[[http~~:~~//www~~.~~uniprot~~.~~org/uniprot/KTHY_HUMAN KTHY_HUMAN]] Catalyzes the conversion of dTMP to dTDP~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[1e98]] 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=1E98 OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Thymidylate kinase\|Thymidylate kinase]]		*[[Thymidylate kinase\|Thymidylate kinase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:011071809</ref><ref group="xtra">PMID:010873853</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]

OCA at 06:22, 16 May 2013

OCA — Thu, 16 May 2013 06:22:45 GMT

←Older revision		Revision as of 06:22, 16 May 2013
Line 1:		Line 1:
-	[[Image:1e98.png\|left\|200px]]
-
	{{STRUCTURE_1e98\| PDB=1e98 \| SCENE= }}		{{STRUCTURE_1e98\| PDB=1e98 \| SCENE= }}
		+	===Wild type human thymidylate kinase complexed with AZTMP and ADP===
		+	{{ABSTRACT_PUBMED_11071809}}

-	===~~WILD TYPE HUMAN THYMIDYLATE KINASE COMPLEXED WITH AZTMP AND ADP~~===	+	==Function==
-		+	[[http://www.uniprot.org/uniprot/KTHY_HUMAN KTHY_HUMAN]] Catalyzes the conversion of dTMP to dTDP.
-	~~{{ABSTRACT_PUBMED_11071809}}~~	+

	==About this Structure==		==About this Structure==
	[[1e98]] 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=1E98 OCA].		[[1e98]] 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=1E98 OCA].
		+
		+	==See Also==
		+	*[[Thymidylate kinase\|Thymidylate kinase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:011071809</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011071809</ref><ref group="xtra">PMID:010873853</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: DTMP kinase]]		[[Category: DTMP kinase]]
Line 25:		Line 27:
	[[Category: P-loop]]		[[Category: P-loop]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]
-	[[Category: ~~Thymidylate kinase~~]]	+	[[Category: Transferase]]