5nrq: Difference between revisions

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'''Unreleased structure'''


The entry 5nrq is ON HOLD
==Mtb TMK crystal structure in complex with compound 33==
<StructureSection load='5nrq' size='340' side='right'caption='[[5nrq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nrq]] 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=5NRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NRQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZUI:1-[1-[[5-(3-chloranylphenoxy)pyridin-3-yl]methyl]piperidin-4-yl]-5-methyl-pyrimidine-2,4-dione'>ZUI</scene></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=5nrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nrq OCA], [https://pdbe.org/5nrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nrq RCSB], [https://www.ebi.ac.uk/pdbsum/5nrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nrq ProSAT]</span></td></tr>
</table>
== Function ==
[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]


Authors: Merceron, R., Song, L., Munier-Lehmann, H., Van Calenbergh, S., Savvides, S.
==See Also==
 
*[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]]
Description: Mtb TMK crystal structure in complex with compound LS3112
__TOC__
[[Category: Unreleased Structures]]
</StructureSection>
[[Category: Song, L]]
[[Category: Large Structures]]
[[Category: Merceron, R]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Van Calenbergh, S]]
[[Category: Merceron R]]
[[Category: Savvides, S]]
[[Category: Munier-Lehmann H]]
[[Category: Munier-Lehmann, H]]
[[Category: Savvides S]]
[[Category: Song L]]
[[Category: Van Calenbergh S]]

Latest revision as of 10:52, 17 January 2024

Mtb TMK crystal structure in complex with compound 33

5nrq, resolution 2.10Å

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