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1uou

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Current revision (12:53, 13 December 2023) (edit) (undo)
 
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<StructureSection load='1uou' size='340' side='right'caption='[[1uou]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
<StructureSection load='1uou' size='340' side='right'caption='[[1uou]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1uou]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UOU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1uou]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UOU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMU:5-CHLORO-6-(1-(2-IMINOPYRROLIDINYL)+METHYL)+URACIL'>CMU</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thymidine_phosphorylase Thymidine phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.4 2.4.2.4] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMU:5-CHLORO-6-(1-(2-IMINOPYRROLIDINYL)+METHYL)+URACIL'>CMU</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=1uou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uou OCA], [https://pdbe.org/1uou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uou RCSB], [https://www.ebi.ac.uk/pdbsum/1uou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uou ProSAT]</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=1uou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uou OCA], [https://pdbe.org/1uou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uou RCSB], [https://www.ebi.ac.uk/pdbsum/1uou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uou ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/TYPH_HUMAN TYPH_HUMAN] Mitochondrial neurogastrointestinal encephalomyopathy. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:9924029</ref> <ref>PMID:12177387</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/TYPH_HUMAN TYPH_HUMAN] May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro.<ref>PMID:1590793</ref> Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.<ref>PMID:1590793</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thymidine phosphorylase]]
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[[Category: Barry ST]]
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[[Category: Barry, S T]]
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[[Category: Bate M]]
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[[Category: Bate, M]]
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[[Category: Breed J]]
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[[Category: Breed, J]]
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[[Category: Colls JG]]
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[[Category: Colls, J G]]
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[[Category: Ernill RJ]]
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[[Category: Ernill, R J]]
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[[Category: Luke RWA]]
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[[Category: Luke, R W.A]]
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[[Category: McAlister MSB]]
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[[Category: McAlister, M S.B]]
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[[Category: McCall EJ]]
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[[Category: McCall, E J]]
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[[Category: McMiken HHJ]]
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[[Category: McMiken, H H.J]]
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[[Category: Minshull CA]]
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[[Category: Minshull, C A]]
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[[Category: Norman RA]]
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[[Category: Norman, R A]]
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[[Category: Paterson DS]]
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[[Category: Paterson, D S]]
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[[Category: Pauptit RA]]
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[[Category: Pauptit, R A]]
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[[Category: Timms D]]
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[[Category: Timms, D]]
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[[Category: Tucker JA]]
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[[Category: Tucker, J A]]
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[[Category: Angiogenesis]]
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[[Category: Chemotaxis]]
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[[Category: Glycosyltransferase]]
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[[Category: Phosphorylase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor

PDB ID 1uou

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