We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

4xr5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:50, 10 January 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==X-ray structure of the unliganded thymidine phosphorylase from Salmonella typhimurium at 2.05 A resolution==
==X-ray structure of the unliganded thymidine phosphorylase from Salmonella typhimurium at 2.05 A resolution==
-
<StructureSection load='4xr5' size='340' side='right' caption='[[4xr5]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
+
<StructureSection load='4xr5' size='340' side='right'caption='[[4xr5]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4xr5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XR5 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4xr5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XR5 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2.05&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x46|4x46]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidine_phosphorylase Thymidine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.4 2.4.2.4] </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=4xr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xr5 OCA], [https://pdbe.org/4xr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xr5 RCSB], [https://www.ebi.ac.uk/pdbsum/4xr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xr5 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=4xr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xr5 OCA], [http://pdbe.org/4xr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xr5 RCSB], [http://www.ebi.ac.uk/pdbsum/4xr5 PDBsum]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://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.
+
[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 24: Line 23:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Thymidine phosphorylase]]
+
[[Category: Large Structures]]
-
[[Category: Balaev, V V]]
+
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-
[[Category: Betzel, C]]
+
[[Category: Balaev VV]]
-
[[Category: Gabdulkhakov, A G]]
+
[[Category: Betzel C]]
-
[[Category: Lashkov, A A]]
+
[[Category: Gabdulkhakov AG]]
-
[[Category: Mikhailov, A M]]
+
[[Category: Lashkov AA]]
-
[[Category: Metabolism]]
+
[[Category: Mikhailov AM]]
-
[[Category: Nucleoside]]
+
-
[[Category: Transferase]]
+

Current revision

X-ray structure of the unliganded thymidine phosphorylase from Salmonella typhimurium at 2.05 A resolution

PDB ID 4xr5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xr5"
Personal tools