1kcw: Difference between revisions

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-[[Image:1kcw.jpg|left|200px]]
- {{Structure
+==X-RAY CRYSTAL STRUCTURE OF HUMAN CERULOPLASMIN AT 3.0 ANGSTROMS==
-|PDB= 1kcw |SIZE=350|CAPTION= <scene name='initialview01'>1kcw</scene>, resolution 3.0&Aring;
+<StructureSection load='1kcw' size='340' side='right'caption='[[1kcw]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
-|SITE= <scene name='pdbsite=CU1:Type+I+Cu+Binding+Site+In+Domain+2.+At+Best+LEU+329+May+...'>CU1</scene>, <scene name='pdbsite=CU2:Type+I+Cu+Binding+Site+In+Domain+4'>CU2</scene>, <scene name='pdbsite=CU3:Labile+Cu+Binding+Site+In+Domain+4'>CU3</scene>, <scene name='pdbsite=CU4:Type+I+Cu+Binding+Site+In+Domain+6'>CU4</scene>, <scene name='pdbsite=CU5:Labile+Cu+Binding+Site+In+Domain+6'>CU5</scene> and <scene name='pdbsite=TRI:Trinuclear+Center.+Cu31+And+32+Are+The+Pair+Of+Type+Iii+...'>TRI</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=O:OXYGEN ATOM'>O</scene>
+<table><tr><td colspan='2'>[[1kcw]] 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=1KCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KCW FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</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=1kcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kcw OCA], [https://pdbe.org/1kcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kcw RCSB], [https://www.ebi.ac.uk/pdbsum/1kcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kcw ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[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.
+== Function ==
+[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).
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kc/1kcw_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kcw ConSurf].
+<div style="clear:both"></div>
-'''X-RAY CRYSTAL STRUCTURE OF HUMAN CERULOPLASMIN AT 3.0 ANGSTROMS'''
+==See Also==
+*[[Ceruloplasmin|Ceruloplasmin]]
+__TOC__
-==Disease==
+</StructureSection>
-Known diseases associated with this structure: Cerebellar ataxia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=117700 117700]], Hemosiderosis, systemic, due to aceruloplasminemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=117700 117700]], Hypoceruloplasminemia, hereditary OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=117700 117700]]
-==About this Structure==
-KCW is a [[Single protein]] structure of 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=1KCW OCA].
-[[Category: Ferroxidase]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Card, G L.]]
+[[Category: Card GL]]
-[[Category: Lindley, P F.]]
+[[Category: Lindley PF]]
-[[Category: Zaitsev, V N.]]
+[[Category: Zaitsev VN]]
-[[Category: CU]]
-[[Category: NAG]]
-[[Category: O]]
-[[Category: ceruloplasmin]]
-[[Category: multi-copper oxidase]]
-[[Category: oxidoreductase]]
-[[Category: plasma protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:15:39 2008''