6nnr: Difference between revisions

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 ==high-resolution structure of wild-type E. coli thymidylate synthase==
-<StructureSection load='6nnr' size='340' side='right' caption='[[6nnr]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
+<StructureSection load='6nnr' size='340' side='right'caption='[[6nnr]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6nnr]] is a 2 chain structure. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4knz 4knz], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4iw5 4iw5] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2g8o 2g8o]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NNR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NNR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6nnr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4knz 4knz], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4iw5 4iw5] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2g8o 2g8o]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NNR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=UMC:2-DEOXY-5-URIDYLIC+ACID'>UMC</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]] 1.05&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CXM:N-CARBOXYMETHIONINE'>CXM</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC+ACID'>CB3</scene>, <scene name='pdbligand=CXM:N-CARBOXYMETHIONINE'>CXM</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=UMC:2-DEOXY-5-URIDYLIC+ACID'>UMC</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=6nnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nnr OCA], [https://pdbe.org/6nnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nnr RCSB], [https://www.ebi.ac.uk/pdbsum/6nnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nnr ProSAT]</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=6nnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nnr OCA], [http://pdbe.org/6nnr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nnr RCSB], [http://www.ebi.ac.uk/pdbsum/6nnr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nnr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TYSY_ECOLI TYSY_ECOLI]] Provides the sole de novo source of dTMP for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation.
+[https://www.uniprot.org/uniprot/TYSY_ECOLI TYSY_ECOLI] Provides the sole de novo source of dTMP for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 19: @@
 </div>
 <div class="pdbe-citations 6nnr" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Thymidylate synthase]]
+[[Category: Escherichia coli K-12]]
-[[Category: Finer-Moore, J]]
+[[Category: Large Structures]]
-[[Category: Stroud, R M]]
+[[Category: Finer-Moore J]]
-[[Category: Cancer drug target]]
+[[Category: Stroud RM]]
-[[Category: Hydride transfer]]
-[[Category: Methyl transfer]]
-[[Category: Nucleotide synthesis]]
-[[Category: Transferase]]