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2e5x

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Current revision (08:35, 25 October 2023) (edit) (undo)
 
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<StructureSection load='2e5x' size='340' side='right'caption='[[2e5x]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2e5x' size='340' side='right'caption='[[2e5x]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2e5x]] is a 1 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=2E5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E5X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2e5x]] is a 1 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=2E5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E5X 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ITT:INOSINE+5-TRIPHOSPHATE'>ITT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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&#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/Nucleoside-triphosphate_diphosphatase Nucleoside-triphosphate diphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.19 3.6.1.19] </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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ITT:INOSINE+5-TRIPHOSPHATE'>ITT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2e5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5x OCA], [https://pdbe.org/2e5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e5x RCSB], [https://www.ebi.ac.uk/pdbsum/2e5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5x ProSAT], [https://www.topsan.org/Proteins/RSGI/2e5x 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=2e5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5x OCA], [https://pdbe.org/2e5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e5x RCSB], [https://www.ebi.ac.uk/pdbsum/2e5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5x ProSAT], [https://www.topsan.org/Proteins/RSGI/2e5x TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NTPA_PYRHO NTPA_PYRHO]] Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP/dITP to their respective monophosphate derivatives. Might exclude non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions (Probable).<ref>PMID:18062990</ref>
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[https://www.uniprot.org/uniprot/IXTPA_PYRHO IXTPA_PYRHO] Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.[HAMAP-Rule:MF_01405]<ref>PMID:18062990</ref>
== 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]]
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[[Category: Nucleoside-triphosphate diphosphatase]]
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[[Category: Pyrococcus horikoshii OT3]]
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[[Category: Pyrococcus horikoshii]]
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[[Category: Kunishima N]]
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[[Category: Kunishima, N]]
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[[Category: Lokanath NK]]
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[[Category: Lokanath, N K]]
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[[Category: Mizutani H]]
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[[Category: Mizutani, H]]
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[[Category: Structural genomic]]
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[[Category: Hydrolase]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Rsgi]]
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Current revision

Structure of nucleotide triphosphate pyrophosphatase from pyrococcus horikoshii OT3

PDB ID 2e5x

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