3h9k
From Proteopedia
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==Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry== | ==Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry== | ||
- | <StructureSection load='3h9k' size='340' side='right' caption='[[3h9k]], [[Resolution|resolution]] 2.65Å' scene=''> | + | <StructureSection load='3h9k' size='340' side='right'caption='[[3h9k]], [[Resolution|resolution]] 2.65Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3h9k]] is a 5 chain structure with sequence from [ | + | <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> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65Å</td></tr> |
- | + | <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> | |
- | <tr id=' | + | <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> |
- | < | + | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/TYSY_HUMAN TYSY_HUMAN] Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.<ref>PMID:21876188</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/3h9k_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/3h9k_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3h9k" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3h9k" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Gibson | + | [[Category: Gibson LM]] |
- | [[Category: Lebioda | + | [[Category: Lebioda L]] |
- | [[Category: Lovelace | + | [[Category: Lovelace LL]] |
- | + | ||
- | + | ||
- | + |
Current revision
Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry
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