1vp2
From Proteopedia
(Difference between revisions)
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<StructureSection load='1vp2' size='340' side='right'caption='[[1vp2]], [[Resolution|resolution]] 1.78Å' scene=''> | <StructureSection load='1vp2' size='340' side='right'caption='[[1vp2]], [[Resolution|resolution]] 1.78Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1vp2]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1vp2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VP2 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1vp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vp2 OCA], [https://pdbe.org/1vp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vp2 RCSB], [https://www.ebi.ac.uk/pdbsum/1vp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vp2 ProSAT], [https://www.topsan.org/Proteins/JCSG/1vp2 TOPSAN]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/IXTPA_THEMA IXTPA_THEMA] 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] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 43589]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Thermotoga maritima]] |
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Revision as of 06:41, 25 January 2023
CRYSTAL STRUCTURE OF A PUTATIVE XANTHOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN HOMOLOG (TM0159) FROM THERMOTOGA MARITIMA AT 1.78 A RESOLUTION
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