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<StructureSection load='6plb' size='340' side='right'caption='[[6plb]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='6plb' size='340' side='right'caption='[[6plb]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6plb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PLB FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PLB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OT1:2-(1-chloranyl-2,3,4,5,6-pentamethyl-1$l^{7}-iridapentacyclo[2.2.0.0^{1,3}.0^{1,5}.0^{2,6}]hexan-1-yl)-1,3-dimethyl-benzimidazole'>OT1</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OT1:2-(1-chloranyl-2,3,4,5,6-pentamethyl-1$l^{7}-iridapentacyclo[2.2.0.0^{1,3}.0^{1,5}.0^{2,6}]hexan-1-yl)-1,3-dimethyl-benzimidazole'>OT1</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=6plb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6plb OCA], [https://pdbe.org/6plb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6plb RCSB], [https://www.ebi.ac.uk/pdbsum/6plb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6plb ProSAT]</span></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=6plb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6plb OCA], [https://pdbe.org/6plb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6plb RCSB], [https://www.ebi.ac.uk/pdbsum/6plb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6plb ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metal complexes can be considered a 'paradigm of promiscuity' when it comes to their reactions with proteins. They often form adducts with a variety of donor atoms in an unselective manner. We have characterized the adducts formed between a series of isostructural N -heterocyclic carbene (NHC) complexes with Ru, Os, Rh, and Ir centers and the model protein hen egg white lysozyme by X-ray crystallography and mass spectrometry. Distinctive behavior for the metal compounds was observed with the more labile Ru and Rh complexes targeting a surface l-histidine moiety through cleavage of p- cymene or NHC co-ligands, respectively. In contrast, the more inert Os and Ir derivatives were detected in an electronegative binding pocket after undergoing ligand exchange of a chlorido ligand for an amino acid side chain. Computational studies supported the binding profiles and hinted at the role of the protein microenvironment for metal complexes eliciting selectivity for specific binding sites on the protein.


Probing the Paradigm of Promiscuity for N-Heterocyclic Carbene Complexes and their Protein Adduct Formation.,Sullivan MP, Cziferszky M, Tolbatov I, Truong D, Mercadante D, Re N, Gust R, Goldstone DC, Hartinger C Angew Chem Int Ed Engl. 2021 Jul 1. doi: 10.1002/anie.202106906. PMID:34196088<ref>PMID:34196088</ref>
==See Also==
 
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6plb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lysozyme]]
[[Category: Goldstone DC]]
[[Category: Goldstone, D C]]
[[Category: Hartinger CG]]
[[Category: Hartinger, C G]]
[[Category: Sullivan MP]]
[[Category: Sullivan, M P]]
[[Category: Anticancer]]
[[Category: Benzimidazole]]
[[Category: Carbene]]
[[Category: Dimethylbenzimidazole]]
[[Category: Hydrolase]]
[[Category: Metal-based]]
[[Category: Metallodrug]]
[[Category: Nhc]]
[[Category: Ruthenium]]

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