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==Mtb TMK crystal structure in complex with compound 1==
==Mtb TMK crystal structure in complex with compound 1==
<StructureSection load='5nq5' size='340' side='right' caption='[[5nq5]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='5nq5' size='340' side='right'caption='[[5nq5]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5nq5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NQ5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5nq5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NQ5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=952:5-methyl-1-[(3~{S})-1-[(3-phenoxyphenyl)methyl]piperidin-3-yl]pyrimidine-2,4-dione'>952</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=952:5-methyl-1-[(3~{S})-1-[(3-phenoxyphenyl)methyl]piperidin-3-yl]pyrimidine-2,4-dione'>952</scene></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=5nq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nq5 OCA], [http://pdbe.org/5nq5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nq5 RCSB], [http://www.ebi.ac.uk/pdbsum/5nq5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nq5 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nq5 OCA], [https://pdbe.org/5nq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nq5 RCSB], [https://www.ebi.ac.uk/pdbsum/5nq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nq5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KTHY_MYCTU KTHY_MYCTU]] Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.[HAMAP-Rule:MF_00165]  
[https://www.uniprot.org/uniprot/KTHY_MYCTU KTHY_MYCTU] Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.[HAMAP-Rule:MF_00165]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5nq5" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5nq5" style="background-color:#fffaf0;"></div>
==See Also==
*[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DTMP kinase]]
[[Category: Large Structures]]
[[Category: Calenbergh, S Van]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Merceron, R]]
[[Category: Merceron R]]
[[Category: Munier-Lehmann, H]]
[[Category: Munier-Lehmann H]]
[[Category: Savvides, S]]
[[Category: Savvides S]]
[[Category: Song, L]]
[[Category: Song L]]
[[Category: Inhibitor]]
[[Category: Van Calenbergh S]]
[[Category: Nucleotide binding]]
[[Category: Thymidylate kinase]]
[[Category: Transferase]]
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