View source for 3eec


==X-ray structure of human ubiquitin Cd(II) adduct==
<StructureSection load='3eec' size='340' side='right' caption='[[3eec]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3eec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EEC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ubq|1ubq]], [[1yj1|1yj1]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPS27A, UBA80, UBCEP1, UBA52, UBCEP2, UBB, UBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3eec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eec OCA], [http://pdbe.org/3eec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eec RCSB], [http://www.ebi.ac.uk/pdbsum/3eec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eec ProSAT]</span></td></tr>
</table>
== 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/ee/3eec_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=3eec ConSurf].
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== Publication Abstract from PubMed ==
A structural investigation performed on adducts of human ubiquitin with group-12 metal ions reveals common preferential anchoring sites, the most populated one being His68; at higher metal ion concentration a second and a third site, close to the N-terminus of the protein, become populated and promote a polymorphic transition from orthorhombic to cubic form; Glu16 and Glu18, involved in the latter metal binding, undergo a remarkable displacement from their position in native ubiquitin; the aggregate stereochemistry appears to be driven by the clustering of deshielded backbone hydrogen-bond patches, and metal ions foster this process.

Structural probing of Zn(ii), Cd(ii) and Hg(ii) binding to human ubiquitin.,Falini G, Fermani S, Tosi G, Arnesano F, Natile G Chem Commun (Camb). 2008 Dec 7;(45):5960-2. Epub 2008 Oct 9. PMID:19030552<ref>PMID:19030552</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3eec" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ubiquitin|Ubiquitin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Arnesano, F]]
[[Category: Falini, G]]
[[Category: Fermani, S]]
[[Category: Natile, G]]
[[Category: Tosi, G]]
[[Category: 3d structure]]
[[Category: Adduct]]
[[Category: Cadmium]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Ubiquitin]]
[[Category: Unknown function]]