4gcd: Difference between revisions

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-'''Unreleased structure'''
-The entry 4gcd is ON HOLD  until Paper Publication
+==Room temperature X-ray diffraction study of a 6-fold molar excess of a cisplatin/carboplatin mixture binding to HEWL, Dataset 2==
+<StructureSection load='4gcd' size='340' side='right'caption='[[4gcd]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4gcd]] 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=4GCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GCD 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=CPT:CISPLATIN'>CPT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</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=4gcd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gcd OCA], [https://pdbe.org/4gcd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gcd RCSB], [https://www.ebi.ac.uk/pdbsum/4gcd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gcd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The anticancer agents cisplatin and carboplatin bind to histidine in a protein. This crystal structure study at data-collection temperatures of 100 and 300 K examines their relative binding affinities to a histidine side chain and the effect of a high X-ray radiation dose of up to approximately 1.8 MGy on the stability of the subsequent protein-Pt adducts. Cisplatin binding is visible at the histidine residue, but carboplatin binding is not. Five refined X-ray crystal structures are presented: one at 100 K as a reference and four at 300 K. The diffraction resolutions are 1.8, 2.0, 2.8, 2.9 and 3.5 A.
-Authors: Helliwell, J.R., Tanley, S.W.M.
+The crystal structure analysis of the relative binding of cisplatin and carboplatin in a mixture with histidine in a protein studied at 100 and 300 K with repeated X-ray irradiation.,Helliwell JR, Tanley SW Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):121-5. doi:, 10.1107/S090744491204423X. Epub 2012 Dec 20. PMID:23275170<ref>PMID:23275170</ref>
-Description: Room temperature X-ray diffraction study of a 6-fold molar excess of a cisplatin/carboplatin mixture binding to HEWL, Dataset 2
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4gcd" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gallus gallus]]
+[[Category: Large Structures]]
+[[Category: Helliwell JR]]
+[[Category: Tanley SWM]]