1wu8: Difference between revisions
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New page: left|200px<br /><applet load="1wu8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wu8, resolution 2.60Å" /> '''Crystal structure of... |
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== | ==Crystal structure of project PH0463 from Pyrococcus horikoshii OT3== | ||
<StructureSection load='1wu8' size='340' side='right'caption='[[1wu8]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
[[ | == Structural highlights == | ||
[[ | <table><tr><td colspan='2'>[[1wu8]] is a 3 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=1WU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WU8 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]] 2.6Å</td></tr> | ||
[[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1wu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wu8 OCA], [https://pdbe.org/1wu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wu8 RCSB], [https://www.ebi.ac.uk/pdbsum/1wu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wu8 ProSAT], [https://www.topsan.org/Proteins/RSGI/1wu8 TOPSAN]</span></td></tr> | ||
[[ | </table> | ||
[[Category: | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/RSAMH_PYRHO RSAMH_PYRHO] Catalyzes the hydrolysis of S-adenosyl-L-methionine (SAM) into adenosine and L-methionine (PubMed:18551689). Is likely stereoselective, specifically hydrolyzing (R)-S-adenosyl-L-methionine ((R)-SAM), the inactive form of the ubiquitous cofactor SAM, and not the active form of SAM, (S)-S-adenosyl-L-methionine (By similarity). Probaly plays a role in preventing accumulation of (R)-S-adenosyl-L-methionine in cells; maintenance of (S)-S-denosyl-L-methionine homochirality is important for cellular health given that the (R)-form is largely inactive as a methyl donor and can function as an inhibitor of methyltransferases (By similarity). Is unable to mediate a fluorination or chlorination reaction with SAM (PubMed:18551689).[UniProtKB:A4X4S2]<ref>PMID:18551689</ref> | ||
[[Category: | == 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/wu/1wu8_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=1wu8 ConSurf]. | |||
<div style="clear:both"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus horikoshii OT3]] | |||
[[Category: Kunishima N]] | |||
[[Category: Shimizu K]] | |||
Latest revision as of 09:42, 25 December 2024
Crystal structure of project PH0463 from Pyrococcus horikoshii OT3
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