1y1t: Difference between revisions

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==Crystal Structure of the Uridine Phosphorylase from Salmonella Typhimurium at 1.77A Resolution==
==Crystal Structure of the Uridine Phosphorylase from Salmonella Typhimurium at 1.77A Resolution==
<StructureSection load='1y1t' size='340' side='right' caption='[[1y1t]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
<StructureSection load='1y1t' size='340' side='right' caption='[[1y1t]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UDP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UDP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_phosphorylase Uridine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.3 2.4.2.3] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_phosphorylase Uridine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.3 2.4.2.3] </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=1y1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1t OCA], [http://pdbe.org/1y1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y1t RCSB], [http://www.ebi.ac.uk/pdbsum/1y1t PDBsum]</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=1y1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1t OCA], [http://pdbe.org/1y1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y1t RCSB], [http://www.ebi.ac.uk/pdbsum/1y1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y1t ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y1t ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Uridine phosphorylase|Uridine phosphorylase]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 17:13, 12 October 2017

Crystal Structure of the Uridine Phosphorylase from Salmonella Typhimurium at 1.77A ResolutionCrystal Structure of the Uridine Phosphorylase from Salmonella Typhimurium at 1.77A Resolution

Structural highlights

1y1t is a 2 chain structure with sequence from Salty. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:UDP (SALTY)
Activity:Uridine phosphorylase, with EC number 2.4.2.3
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UDP_SALTY] Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1y1t, resolution 1.77Å

Drag the structure with the mouse to rotate

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OCA