4ges: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4ges]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GES FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0WZ:3-(1H-PYRAZOL-1-YL)-L-TYROSINE'>0WZ</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.23&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0WZ:3-(1H-PYRAZOL-1-YL)-L-TYROSINE'>0WZ</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=4ges FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ges OCA], [https://pdbe.org/4ges PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ges RCSB], [https://www.ebi.ac.uk/pdbsum/4ges PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ges ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-ET encounters jellyfish: Through the incorporation of the metal-chelating amino acid pyTyr into green fluorescent protein (GFP) from jellyfish, photoinduced electron transfer (ET) from the GFP chromophore to a bound Cu(II) ion was shown to occur within one nanosecond in a distance-dependent manner. The crystal structure of GFP with pyTyr at a specific position shows the structural basis for the nanomolar binding affinity of pyTyr to Cu(II) ions.
-Genetic incorporation of a metal-chelating amino Acid as a probe for protein electron transfer.,Liu X, Li J, Dong J, Hu C, Gong W, Wang J Angew Chem Int Ed Engl. 2012 Oct 8;51(41):10261-5. doi: 10.1002/anie.201204962., Epub 2012 Aug 31. PMID:22936654<ref>PMID:22936654</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ges" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>