View source for 3bf5


==Crystal structure of putative ribokinase (10640157) from Thermoplasma acidophilum at 1.91 A resolution==
<StructureSection load='3bf5' size='340' side='right'caption='[[3bf5]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bf5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum_DSM_1728 Thermoplasma acidophilum DSM 1728]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BF5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3bf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bf5 OCA], [https://pdbe.org/3bf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bf5 RCSB], [https://www.ebi.ac.uk/pdbsum/3bf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bf5 ProSAT], [https://www.topsan.org/Proteins/JCSG/3bf5 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NK_THEAC NK_THEAC] Nucleoside kinase with broad substrate specificity. Catalyzes the phosphorylation of a variety of nucleosides to the corresponding nucleoside 5'-mono-phosphate in the presence of phosphate donors and divalent cations. Displays the most efficient activity with guanosine, followed by inosine, cytidine, and adenosine. Negligible enzymatic activity is detected with thymidine, uridine, and 2-deoxyadenosine. ATP is the most efficient phosphate donor, but can also use GTP and ITP. Shows no sugar kinase activity, since it is unable to phosphorylate ribose, fructose-1-phosphate, or fructose-6-phosphate.<ref>PMID:23161756</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/3bf5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=3bf5 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermoplasma acidophilum DSM 1728]]