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1vmk
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1vmk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vmk, resolution 2.01Å" /> '''Crystal structure of...) |
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| - | [[Image:1vmk.gif|left|200px]]<br /><applet load="1vmk" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1vmk, resolution 2.01Å" /> | ||
| - | '''Crystal structure of Purine nucleoside phosphorylase (TM1596) from Thermotoga maritima at 2.01 A resolution'''<br /> | ||
| - | == | + | ==Crystal structure of Purine nucleoside phosphorylase (TM1596) from Thermotoga maritima at 2.01 A resolution== |
| - | + | <StructureSection load='1vmk' size='340' side='right'caption='[[1vmk]], [[Resolution|resolution]] 2.01Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1vmk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VMK 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]] 2.01Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GUN:GUANINE'>GUN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1vmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vmk OCA], [https://pdbe.org/1vmk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vmk RCSB], [https://www.ebi.ac.uk/pdbsum/1vmk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vmk ProSAT], [https://www.topsan.org/Proteins/JCSG/1vmk TOPSAN]</span></td></tr> |
| - | [ | + | </table> |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/Q9X1T2_THEMA Q9X1T2_THEMA] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (By similarity).[PIRNR:PIRNR000477] |
| - | + | == 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/vm/1vmk_consurf.spt"</scriptWhenChecked> | |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1vmk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga maritima MSB8]] | ||
Current revision
Crystal structure of Purine nucleoside phosphorylase (TM1596) from Thermotoga maritima at 2.01 A resolution
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