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==Crystal structure of human uridine phosphorylase 2== | ==Crystal structure of human uridine phosphorylase 2== | ||
<StructureSection load='2xrf' size='340' side='right' caption='[[2xrf]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2xrf' size='340' side='right' caption='[[2xrf]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=URA:URACIL'>URA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=URA:URACIL'>URA</scene></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=2xrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xrf RCSB], [http://www.ebi.ac.uk/pdbsum/2xrf 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=2xrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrf OCA], [http://pdbe.org/2xrf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xrf RCSB], [http://www.ebi.ac.uk/pdbsum/2xrf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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=2xrf ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
Revision as of 04:31, 5 August 2016
Crystal structure of human uridine phosphorylase 2Crystal structure of human uridine phosphorylase 2
Structural highlights
Function[UPP2_HUMAN] 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. Shows substrate specificity and accept uridine, deoxyuridine, and thymidine as well as the two pyrimidine nucleoside analogs 5-fluorouridine and 5-fluoro-2(')-deoxyuridine as substrates. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Human
- Uridine phosphorylase
- Arrowsmith, C H
- Berg, S Van Der
- Berglund, H
- Bountra, C
- Collins, R
- Edwards, A M
- Flodin, S
- Flores, A
- Graslund, S
- Hammarstrom, M
- Johansson, I
- Karlberg, T
- Kol, S
- Kotenyova, T
- Kouznetsova, E
- Moche, M
- Nordlund, P
- Nyman, T
- Persson, C
- Schuler, H
- Schutz, P
- Siponen, M I
- Thorsell, A G
- Tresaugues, L
- Wahlberg, E
- Weigelt, J
- Welin, M
- Transferase