2cze: Difference between revisions

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<StructureSection load='2cze' size='340' side='right'caption='[[2cze]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='2cze' size='340' side='right'caption='[[2cze]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cze]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CZE FirstGlance]. <br>
<table><tr><td colspan='2'>[[2cze]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CZE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</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]] 1.85&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cz5|2cz5]], [[2czd|2czd]], [[2czf|2czf]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pyrF, PH0731 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] </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=2cze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cze OCA], [https://pdbe.org/2cze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cze RCSB], [https://www.ebi.ac.uk/pdbsum/2cze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cze ProSAT], [https://www.topsan.org/Proteins/RSGI/2cze TOPSAN]</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=2cze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cze OCA], [https://pdbe.org/2cze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cze RCSB], [https://www.ebi.ac.uk/pdbsum/2cze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cze ProSAT], [https://www.topsan.org/Proteins/RSGI/2cze TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PYRF_PYRHO PYRF_PYRHO]] Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) (By similarity).[HAMAP-Rule:MF_01200_A]  
[https://www.uniprot.org/uniprot/PYRF_PYRHO PYRF_PYRHO] Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) (By similarity).[HAMAP-Rule:MF_01200_A]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Orotidine-5'-phosphate decarboxylase]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Pyrococcus horikoshii]]
[[Category: Arai R]]
[[Category: Arai, R]]
[[Category: Ito K]]
[[Category: Ito, K]]
[[Category: Kishishita S]]
[[Category: Kishishita, S]]
[[Category: Shirouzu M]]
[[Category: Structural genomic]]
[[Category: Yokoyama S]]
[[Category: Shirouzu, M]]
[[Category: Yokoyama, S]]
[[Category: Lyase]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Pyrimidine biosynthesis]]
[[Category: Rsgi]]
[[Category: Ump]]

Latest revision as of 11:21, 25 October 2023

Crystal structure of orotidine 5'-phosphate decarboxylase from Pyrococcus horikoshii OT3 complexed with UMPCrystal structure of orotidine 5'-phosphate decarboxylase from Pyrococcus horikoshii OT3 complexed with UMP

Structural highlights

2cze is a 2 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

PYRF_PYRHO Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) (By similarity).[HAMAP-Rule:MF_01200_A]

Evolutionary Conservation

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

See Also

2cze, resolution 1.85Å

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