3h9k

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[[Image:3h9k.png|left|200px]]
 
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==Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry==
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The line below this paragraph, containing "STRUCTURE_3h9k", creates the "Structure Box" on the page.
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<StructureSection load='3h9k' size='340' side='right'caption='[[3h9k]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3h9k]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H9K FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UFP:5-FLUORO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>UFP</scene></td></tr>
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{{STRUCTURE_3h9k| PDB=3h9k | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h9k OCA], [https://pdbe.org/3h9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h9k RCSB], [https://www.ebi.ac.uk/pdbsum/3h9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h9k ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TYSY_HUMAN TYSY_HUMAN] Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.<ref>PMID:21876188</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/3h9k_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h9k ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Thymidylate synthase (TS) is a well validated target in cancer chemotherapy. Here, a new crystal form of the R163K variant of human TS (hTS) with five subunits per asymmetric part of the unit cell, all with loop 181-197 in the active conformation, is reported. This form allows binding studies by soaking crystals in artificial mother liquors containing ligands that bind in the active site. Using this approach, crystal structures of hTS complexes with FdUMP and dUMP were obtained, indicating that this form should facilitate high-throughput analysis of hTS complexes with drug candidates. Crystal soaking experiments using oxidized glutathione revealed that hTS binds this ligand. Interestingly, the two types of binding observed are both asymmetric. In one subunit of the physiological dimer covalent modification of the catalytic nucleophile Cys195 takes place, while in another dimer a noncovalent adduct with reduced glutathione is formed in one of the active sites.
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===Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry===
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Structures of human thymidylate synthase R163K with dUMP, FdUMP and glutathione show asymmetric ligand binding.,Gibson LM, Celeste LR, Lovelace LL, Lebioda L Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):60-6. Epub 2010 Dec 16. PMID:21206062<ref>PMID:21206062</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3h9k" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[3h9k]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H9K OCA].
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*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Thymidylate synthase]]
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[[Category: Large Structures]]
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[[Category: Gibson, L M.]]
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[[Category: Gibson LM]]
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[[Category: Lebioda, L.]]
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[[Category: Lebioda L]]
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[[Category: Lovelace, L L.]]
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[[Category: Lovelace LL]]

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Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry

PDB ID 3h9k

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