5hmj

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==Re-refinement of 4xan: hen lysozyme with carboplatin in sodium bromide solution==
==Re-refinement of 4xan: hen lysozyme with carboplatin in sodium bromide solution==
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<StructureSection load='5hmj' size='340' side='right' caption='[[5hmj]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='5hmj' size='340' side='right'caption='[[5hmj]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hmj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4xan 4xan] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4nsf 4nsf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HMJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hmj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4xan 4xan] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4nsf 4nsf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HMJ 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</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]] 1.299901&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xan|4xan]]</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</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=5hmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hmj OCA], [https://pdbe.org/5hmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hmj RCSB], [https://www.ebi.ac.uk/pdbsum/5hmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hmj 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=5hmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hmj OCA], [http://pdbe.org/5hmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hmj RCSB], [http://www.ebi.ac.uk/pdbsum/5hmj PDBsum]</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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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The platinum anti-cancer agents cisplatin and carboplatin bind to the histidine 15 residue in the model protein hen egg white lysozyme. By using temperatures either side of the protein glass transition state ( approximately 180 K), several platinum binding modes are seen and show that not all these platinum modes are stable. In particular, the mean square displacement vibration amplitudes of the cisplatin and of the histidine to which it is bound are analysed in detail. As well as the multiple platinum peaks, the electron density for the His-15 side chain is weak to absent at 150 K and 200 K, which points to the imidazole ring of the His side chain sampling multiple positions. Most interestingly, the His-15 imidazole becomes more ordered at room temperature.
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A re-refinement of 4xan, hen egg-white lysozyme (HEWL) with carboplatin crystallized in NaBr solution, has been made and is published here as an addendum to Tanley et al. [(2014), Acta Cryst. F70, 1135-1142]. This follows a previous re-refinement and PDB deposition (4yem) by Shabalin et al. [(2015), Acta Cryst. D71, 1965-1979]. The critical evaluation of the original PDB deposition (4xan), and the subsequent critical examination of the re-refined structure (4yem), has led to an improved model (PDB code 5hmj).
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Structural dynamics of cisplatin binding to histidine in a protein.,Tanley SW, Helliwell JR Struct Dyn. 2014 Jun 17;1(3):034701. doi: 10.1063/1.4883975. eCollection 2014, May. PMID:26798779<ref>PMID:26798779</ref>
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Re-refinement of 4xan: hen egg-white lysozyme with carboplatin in sodium bromide solution.,Tanley SW, Schreurs AM, Kroon-Batenburg LM, Helliwell JR Acta Crystallogr F Struct Biol Commun. 2016 Mar 1;72(Pt 3):251-252. Epub 2016 Feb, 19. PMID:26919531<ref>PMID:26919531</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 5hmj" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5hmj" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
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[[Category: Helliwell, J R]]
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[[Category: Helliwell JR]]
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[[Category: Carboplatin]]
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[[Category: Hen egg white lysozyme]]
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[[Category: Histidine]]
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[[Category: Hydrolase]]
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[[Category: Nabr]]
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Re-refinement of 4xan: hen lysozyme with carboplatin in sodium bromide solution

PDB ID 5hmj

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