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3v5z

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==Structure of FBXL5 hemerythrin domain, C2 cell, grown anaerobically==
==Structure of FBXL5 hemerythrin domain, C2 cell, grown anaerobically==
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<StructureSection load='3v5z' size='340' side='right' caption='[[3v5z]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
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<StructureSection load='3v5z' size='340' side='right'caption='[[3v5z]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3v5z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V5Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V5Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3v5z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V5Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v5x|3v5x]], [[3v5y|3v5y]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v5x|3v5x]], [[3v5y|3v5y]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBL4, FBL5, FBXL5, FLR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBL4, FBL5, FBXL5, FLR1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=3v5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v5z OCA], [http://pdbe.org/3v5z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v5z RCSB], [http://www.ebi.ac.uk/pdbsum/3v5z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v5z ProSAT]</span></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=3v5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v5z OCA], [https://pdbe.org/3v5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v5z RCSB], [https://www.ebi.ac.uk/pdbsum/3v5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v5z ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FBXL5_HUMAN FBXL5_HUMAN]] Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued.<ref>PMID:17532294</ref> <ref>PMID:19762596</ref> <ref>PMID:19762597</ref>
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[[https://www.uniprot.org/uniprot/FBXL5_HUMAN FBXL5_HUMAN]] Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued.<ref>PMID:17532294</ref> <ref>PMID:19762596</ref> <ref>PMID:19762597</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Brautigam, C A]]
[[Category: Brautigam, C A]]
[[Category: Bruick, R K]]
[[Category: Bruick, R K]]

Revision as of 08:33, 20 July 2022

Structure of FBXL5 hemerythrin domain, C2 cell, grown anaerobically

PDB ID 3v5z

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