5nrq

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'''Unreleased structure'''
 
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The entry 5nrq is ON HOLD until Jul 24 2019
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==Mtb TMK crystal structure in complex with compound 33==
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<StructureSection load='5nrq' size='340' side='right' caption='[[5nrq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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Authors: Merceron, R., Song, L., Munier-Lehmann, H., Van Calenbergh, S., Savvides, S.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5nrq]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NRQ FirstGlance]. <br>
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Description: Mtb TMK crystal structure in complex with compound 33
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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[[Category: Unreleased Structures]]
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<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>
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[[Category: Van Calenbergh, S]]
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<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=5nrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nrq OCA], [http://pdbe.org/5nrq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nrq RCSB], [http://www.ebi.ac.uk/pdbsum/5nrq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nrq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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]
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__TOC__
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</StructureSection>
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[[Category: DTMP kinase]]
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[[Category: Calenbergh, S Van]]
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[[Category: Merceron, R]]
[[Category: Munier-Lehmann, H]]
[[Category: Munier-Lehmann, H]]
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[[Category: Savvides, S]]
[[Category: Song, L]]
[[Category: Song, L]]
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[[Category: Savvides, S]]
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[[Category: Inhibitor]]
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[[Category: Merceron, R]]
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[[Category: Nucleotide binding]]
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[[Category: Thymidylate kinase]]
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[[Category: Transferase]]

Revision as of 21:13, 9 August 2018

Mtb TMK crystal structure in complex with compound 33

5nrq, resolution 2.10Å

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