4enz: Difference between revisions

No edit summary
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:


==Structure of human ceruloplasmin at 2.6 A resolution==
==Structure of human ceruloplasmin at 2.6 A resolution==
<StructureSection load='4enz' size='340' side='right' caption='[[4enz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='4enz' size='340' side='right'caption='[[4enz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ENZ FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ejx|4ejx]]</td></tr>
<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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=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>
<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=4enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enz OCA], [http://pdbe.org/4enz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4enz RCSB], [http://www.ebi.ac.uk/pdbsum/4enz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4enz ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[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.  
[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 ==
== Function ==
[[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).  
[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).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 29: Line 28:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ferroxidase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bartunik, H]]
[[Category: Large Structures]]
[[Category: Bourenkov, G]]
[[Category: Bartunik H]]
[[Category: Samygina, V R]]
[[Category: Bourenkov G]]
[[Category: Sokolov, A V]]
[[Category: Samygina VR]]
[[Category: Vasilyev, V B]]
[[Category: Sokolov AV]]
[[Category: Oxidoreductase]]
[[Category: Vasilyev VB]]
[[Category: Plastocyanin-like domain]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA