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5n0k

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'''Unreleased structure'''
 
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The entry 5n0k is ON HOLD until Paper Publication
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==Rat ceruloplasmin orthorhombic form==
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<StructureSection load='5n0k' size='340' side='right'caption='[[5n0k]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5n0k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N0K FirstGlance]. <br>
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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]] 2.3&#8491;</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5n0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n0k OCA], [https://pdbe.org/5n0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n0k RCSB], [https://www.ebi.ac.uk/pdbsum/5n0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n0k ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CERU_RAT CERU_RAT] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. May also play a role in fetal lung development or pulmonary antioxidant defense. involved in iron transport across the cell membrane (By similarity). Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1.<ref>PMID:14707133</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ceruloplasmin (Cp) is a copper-containing multifunctional oxidase of plasma, an antioxidant, an acute-phase protein and a free radical scavenger. The structural organization of Cp causes its sensitivity to proteolysis and ROS (reactive oxygen species), which can alter some of the important Cp functions. Elucidation of the orthorhombic crystal structure of rat Cp at 2.3 A resolution revealed the basis for stronger resistance of rat Cp to proteolysis and a new labile copper binding site. The presence of this site appears as a very rare and distinctive feature of rat Cp as was shown by sequence alignment of ceruloplasmin, hephaestin and zyklopen in the Deuterostomia taxonomic group. The trigonal crystal form of rat Cp at 3.2 A demonstrates unexpected partial substitution of copper by zinc.
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Authors: Samygina, V.R., Sokolov, A.V., Bourenkov, G., Vasilyev, V.B.
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Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic.,Samygina VR, Sokolov AV, Bourenkov G, Schneider TR, Anashkin VA, Kozlov SO, Kolmakov NN, Vasilyev VB Metallomics. 2017 Nov 27. doi: 10.1039/c7mt00157f. PMID:29177316<ref>PMID:29177316</ref>
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Description: Rat ceruloplasmin orthorhombic form
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Sokolov, A.V]]
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<div class="pdbe-citations 5n0k" style="background-color:#fffaf0;"></div>
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[[Category: Bourenkov, G]]
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[[Category: Vasilyev, V.B]]
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==See Also==
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[[Category: Samygina, V.R]]
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*[[Ceruloplasmin|Ceruloplasmin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Rattus norvegicus]]
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[[Category: Bourenkov G]]
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[[Category: Samygina VR]]
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[[Category: Sokolov AV]]
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[[Category: Vasilyev VB]]

Current revision

Rat ceruloplasmin orthorhombic form

PDB ID 5n0k

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