5n27
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of human heavy chain ferritin (apo form)== | |
| + | <StructureSection load='5n27' size='340' side='right' caption='[[5n27]], [[Resolution|resolution]] 1.74Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5n27]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N27 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N27 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5n27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n27 OCA], [http://pdbe.org/5n27 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n27 RCSB], [http://www.ebi.ac.uk/pdbsum/5n27 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n27 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The aim of this work is to identify the cisplatin binding sites on human H-chain ferritin. High-resolution X-ray crystallography reveals that cisplatin binds four distinct protein sites, that is, the side chains of His136 and Lys68, the side chain of His105, the side chain of Cys90 and the side chain of Cys102. These Pt binding sites are compared with those observed for the adduct that cisplatin forms upon encapsulation within horse spleen L-chain ferritin (87% identity with human L-chain ferritin). | ||
| - | + | Cisplatin Binding Sites in Human H-Chain Ferritin.,Ferraro G, Ciambellotti S, Messori L, Merlino A Inorg Chem. 2017 Jul 24. doi: 10.1021/acs.inorgchem.7b01072. PMID:28737381<ref>PMID:28737381</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5n27" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ferroxidase]] | ||
[[Category: Ferraro, G]] | [[Category: Ferraro, G]] | ||
[[Category: Merlino, A]] | [[Category: Merlino, A]] | ||
| + | [[Category: Ferritin]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 04:03, 4 August 2017
X-ray structure of human heavy chain ferritin (apo form)
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