1ky5: Difference between revisions

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-[[Image:1ky5.png|left|200px]]
-{{STRUCTURE_1ky5|  PDB=1ky5  |  SCENE=  }}
+==D244E mutant S-Adenosylhomocysteine hydrolase refined with noncrystallographic restraints==
+<StructureSection load='1ky5' size='340' side='right'caption='[[1ky5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ky5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KY5 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]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADY:3-OXO-ADENOSINE'>ADY</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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=1ky5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky5 OCA], [https://pdbe.org/1ky5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ky5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ky5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ky5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SAHH_RAT SAHH_RAT] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
+== 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/ky/1ky5_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=1ky5 ConSurf].
+<div style="clear:both"></div>
-===D244E mutant S-Adenosylhomocysteine hydrolase refined with noncrystallographic restraints===
+==See Also==
+*[[S-adenosylhomocysteine hydrolase|S-adenosylhomocysteine hydrolase]]
-{{ABSTRACT_PUBMED_11927587}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[1ky5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY5 OCA].
-==Reference==
-<ref group="xtra">PMID:011927587</ref><references group="xtra"/>
-[[Category: Adenosylhomocysteinase]]
 [[Category: Rattus norvegicus]]
-[[Category: Takata, Y.]]
+[[Category: Takata Y]]
-[[Category: Takusagawa, F.]]
+[[Category: Takusagawa F]]
-[[Category: Hydrolase]]
-[[Category: S-adenosylhomocysteine]]