5nrn: Difference between revisions
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==Mtb TMK crystal structure in complex with compound 3== | |||
<StructureSection load='5nrn' size='340' side='right' caption='[[5nrn]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== 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> | |||
</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> | |||
[[Category: | <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=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> | |||
</table> | |||
== 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] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: DTMP kinase]] | |||
[[Category: Calenbergh, S Van]] | |||
[[Category: Merceron, R]] | |||
[[Category: Munier-Lehmann, H]] | |||
[[Category: Savvides, S]] | |||
[[Category: Song, L]] | |||
[[Category: Inhibitor]] | |||
[[Category: Nucleotide binding]] | |||
[[Category: Thymidylate kinase]] | |||
[[Category: Transferase]] | |||
Revision as of 00:13, 10 August 2018
Mtb TMK crystal structure in complex with compound 3Mtb TMK crystal structure in complex with compound 3
Structural highlights
Function[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] |
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