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4gcc

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<StructureSection load='4gcc' size='340' side='right'caption='[[4gcc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4gcc' size='340' side='right'caption='[[4gcc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gcc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GCC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gcc]] 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=4GCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GCC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CPT:CISPLATIN'>CPT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
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</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dd0|4dd0]], [[4dd1|4dd1]], [[4dd2|4dd2]], [[4dd3|4dd3]], [[4dd4|4dd4]], [[4dd6|4dd6]], [[4dd7|4dd7]], [[4dd9|4dd9]], [[4dda|4dda]], [[4ddb|4ddb]], [[4ddc|4ddc]], [[4g49|4g49]], [[4g4a|4g4a]], [[4g4b|4g4b]], [[4g4c|4g4c]], [[4g4h|4g4h]], [[4gcb|4gcb]], [[4gcd|4gcd]], [[4gce|4gce]], [[4gcf|4gcf]], [[4gcj|4gcj]]</td></tr>
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<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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gcc OCA], [https://pdbe.org/4gcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gcc RCSB], [https://www.ebi.ac.uk/pdbsum/4gcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gcc ProSAT]</span></td></tr>
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<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=4gcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gcc OCA], [http://pdbe.org/4gcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gcc RCSB], [http://www.ebi.ac.uk/pdbsum/4gcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gcc ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4gcc" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lysozyme]]
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[[Category: Helliwell JR]]
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[[Category: Helliwell, J R]]
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[[Category: Tanley SWM]]
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[[Category: Tanley, S W.M]]
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[[Category: Binding occupancy]]
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[[Category: Carboplatin]]
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[[Category: Cisplatin]]
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[[Category: Histidine]]
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[[Category: Hydrolase]]
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[[Category: Radiation therapy]]
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[[Category: Relative toxicity]]
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[[Category: Temperature variation and structure]]
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[[Category: X-ray radiation damage]]
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Current revision

Room temperature X-ray diffraction study of a 6-fold molar excess of a cisplatin/carboplatin mixture binding to HEWL, Dataset 1

PDB ID 4gcc

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