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==X-ray structure of the thymidine phosphorylase from Salmonella typhimurium in complex with cytidine and sulphate== | ==X-ray structure of the thymidine phosphorylase from Salmonella typhimurium in complex with cytidine and sulphate== | ||
<StructureSection load='5ey3' size='340' side='right' caption='[[5ey3]], [[Resolution|resolution]] 1.91Å' scene=''> | <StructureSection load='5ey3' size='340' side='right'caption='[[5ey3]], [[Resolution|resolution]] 1.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ey3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EY3 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5ey3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EY3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CTN:4-AMINO-1-BETA-D-RIBOFURANOSYL-2(1H)-PYRIMIDINONE'>CTN</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.905Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CTN:4-AMINO-1-BETA-D-RIBOFURANOSYL-2(1H)-PYRIMIDINONE'>CTN</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ey3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ey3 OCA], [https://pdbe.org/5ey3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ey3 RCSB], [https://www.ebi.ac.uk/pdbsum/5ey3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ey3 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/TYPH_SALTY TYPH_SALTY] The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | ||
[[Category: | [[Category: Balaev VV]] | ||
[[Category: | [[Category: Betzel C]] | ||
[[Category: | [[Category: Gabdulkhakov AG]] | ||
[[Category: | [[Category: Lashkov AA]] | ||
[[Category: | [[Category: Mikhailov AM]] | ||
Latest revision as of 11:32, 12 July 2023
X-ray structure of the thymidine phosphorylase from Salmonella typhimurium in complex with cytidine and sulphateX-ray structure of the thymidine phosphorylase from Salmonella typhimurium in complex with cytidine and sulphate
Structural highlights
FunctionTYPH_SALTY The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. |
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