6auj: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
m Protected "6auj" [edit=sysop:move=sysop]
OCA (talk | contribs)
No edit summary
 
Line 1: Line 1:


==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]] 1.70&Aring;' scene=''>
<StructureSection load='6auj' size='340' side='right'caption='[[6auj]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6auj]] is a 3 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AUJ FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M0H:S-(HYDROXYMETHYL)-L-CYSTEINE'>M0H</scene></td></tr>
<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">thyA, BD94_0762 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1338011 Elizabethkingia anophelis NUHP1])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] </span></td></tr>
<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=6auj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6auj OCA], [http://pdbe.org/6auj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6auj RCSB], [http://www.ebi.ac.uk/pdbsum/6auj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6auj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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]  
[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]
 
==See Also==
*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Elizabethkingia anophelis nuhp1]]
[[Category: Elizabethkingia anophelis NUHP1]]
[[Category: Thymidylate synthase]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Elizabethkingia anopheli]]
[[Category: Ssgcid]]
[[Category: Transferase]]

Latest revision as of 14:25, 4 October 2023

Crystal structure of thymidylate synthase from Elizabethkingia anophelis NUHP1

6auj, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA