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6auj
From Proteopedia
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==Crystal structure of thymidylate synthase from Elizabethkingia anophelis NUHP1== | ==Crystal structure of thymidylate synthase from Elizabethkingia anophelis NUHP1== | ||
| - | <StructureSection load='6auj' size='340' side='right' caption='[[6auj]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='6auj' size='340' side='right'caption='[[6auj]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6auj]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6auj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_anophelis_NUHP1 Elizabethkingia anophelis NUHP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AUJ 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]] 1.7Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M0H:S-(HYDROXYMETHYL)-L-CYSTEINE'>M0H</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=6auj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6auj OCA], [https://pdbe.org/6auj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6auj RCSB], [https://www.ebi.ac.uk/pdbsum/6auj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6auj 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/A0A077EAN3_9FLAO A0A077EAN3_9FLAO] Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.[HAMAP-Rule:MF_00008] |
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| + | ==See Also== | ||
| + | *[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Elizabethkingia anophelis | + | [[Category: Elizabethkingia anophelis NUHP1]] |
| - | [[Category: | + | [[Category: Large Structures]] |
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Current revision
Crystal structure of thymidylate synthase from Elizabethkingia anophelis NUHP1
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