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==Mtb TMK crystal structure in complex with compound 3==
==Mtb TMK crystal structure in complex with compound 3==
<StructureSection load='5nrn' size='340' side='right' caption='[[5nrn]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5nrn' size='340' side='right'caption='[[5nrn]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5nrn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NRN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NRN FirstGlance]. <br>
<table><tr><td colspan='2'>[[5nrn]] is a 2 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=5NRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NRN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=95W:5-methyl-1-[1-[(6-phenoxypyridin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4-dione'>95W</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.2&#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=95W:5-methyl-1-[1-[(6-phenoxypyridin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4-dione'>95W</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5nrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nrn OCA], [http://pdbe.org/5nrn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nrn RCSB], [http://www.ebi.ac.uk/pdbsum/5nrn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nrn 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=5nrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nrn OCA], [https://pdbe.org/5nrn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nrn RCSB], [https://www.ebi.ac.uk/pdbsum/5nrn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nrn 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]
 
==See Also==
*[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]]
__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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