1w2g: Difference between revisions

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 <StructureSection load='1w2g' size='340' side='right'caption='[[1w2g]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1w2g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W2G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1w2g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W2G FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=THM:THYMIDINE'>THM</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]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g3u|1g3u]], [[1gsi|1gsi]], [[1gtv|1gtv]], [[1mrn|1mrn]], [[1mrs|1mrs]], [[1n5i|1n5i]], [[1n5j|1n5j]], [[1n5k|1n5k]], [[1n5l|1n5l]], [[1w2h|1w2h]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=THM:THYMIDINE'>THM</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=1w2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w2g OCA], [https://pdbe.org/1w2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w2g RCSB], [https://www.ebi.ac.uk/pdbsum/1w2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w2g 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=1w2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w2g OCA], [http://pdbe.org/1w2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w2g RCSB], [http://www.ebi.ac.uk/pdbsum/1w2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w2g ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KTHY_MYCTU KTHY_MYCTU]] Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.[HAMAP-Rule:MF_00165]
+[https://www.uniprot.org/uniprot/KTHY_MYCTU KTHY_MYCTU] Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.[HAMAP-Rule:MF_00165]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 ==See Also==
-*[[Thymidylate kinase|Thymidylate kinase]]
+*[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: DTMP kinase]]
-[[Category: Adam, V]]
-[[Category: Bourgeois, D]]
-[[Category: Fioravanti, E]]
-[[Category: Munier-Lehmann, H]]
-[[Category: Azt]]
-[[Category: Inhibition mechanism]]
 [[Category: Mycobacterium tuberculosis]]
-[[Category: Thymidylate kinase]]
+[[Category: Adam V]]
-[[Category: Transferase]]
+[[Category: Bourgeois D]]
+[[Category: Fioravanti E]]
+[[Category: Munier-Lehmann H]]