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4enz

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{{STRUCTURE_4enz| PDB=4enz | SCENE= }}
 
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===Structure of human ceruloplasmin at 2.6 A resolution===
 
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{{ABSTRACT_PUBMED_23843990}}
 
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==Disease==
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==Structure of human ceruloplasmin at 2.6 A resolution==
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[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[http://omim.org/entry/604290 604290]]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.
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<StructureSection load='4enz' size='340' side='right'caption='[[4enz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[4enz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ENZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ENZ FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] 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. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
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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]] 2.6&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
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==About this Structure==
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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=4enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enz OCA], [https://pdbe.org/4enz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4enz RCSB], [https://www.ebi.ac.uk/pdbsum/4enz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4enz ProSAT]</span></td></tr>
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[[4enz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ENZ OCA].
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[https://omim.org/entry/604290 604290]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.
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== Function ==
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[https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN] 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. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
==See Also==
==See Also==
*[[Ceruloplasmin|Ceruloplasmin]]
*[[Ceruloplasmin|Ceruloplasmin]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:023843990</ref><references group="xtra"/><references/>
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[[Category: Ferroxidase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bartunik, H.]]
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[[Category: Large Structures]]
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[[Category: Bourenkov, G.]]
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[[Category: Bartunik H]]
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[[Category: Samygina, V R.]]
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[[Category: Bourenkov G]]
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[[Category: Sokolov, A V.]]
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[[Category: Samygina VR]]
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[[Category: Vasilyev, V B.]]
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[[Category: Sokolov AV]]
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[[Category: Oxidoreductase]]
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[[Category: Vasilyev VB]]
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[[Category: Plastocyanin-like domain]]
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Current revision

Structure of human ceruloplasmin at 2.6 A resolution

PDB ID 4enz

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