6zlq
From Proteopedia
(Difference between revisions)
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==Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor== | ==Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor== | ||
| - | <StructureSection load='6zlq' size='340' side='right'caption='[[6zlq]]' scene=''> | + | <StructureSection load='6zlq' size='340' side='right'caption='[[6zlq]], [[Resolution|resolution]] 3.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZLQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zlq]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZLQ FirstGlance]. <br> |
| - | </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=6zlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zlq OCA], [https://pdbe.org/6zlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zlq RCSB], [https://www.ebi.ac.uk/pdbsum/6zlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zlq ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6zh5|6zh5]], [[6zlg|6zlg]], [[6z3d|6z3d]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ftl1, Ftl1-ps1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=6zlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zlq OCA], [https://pdbe.org/6zlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zlq RCSB], [https://www.ebi.ac.uk/pdbsum/6zlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zlq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/Q9CPX4_MOUSE Q9CPX4_MOUSE]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.[RuleBase:RU361145] | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ferritin 3D structures|Ferritin 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Abelya G]] | + | [[Category: Lk3 transgenic mice]] |
| - | [[Category: Davidov G]] | + | [[Category: Abelya, G]] |
| - | [[Category: Frank | + | [[Category: Davidov, G]] |
| - | [[Category: | + | [[Category: Frank, G A]] |
| - | [[Category: | + | [[Category: Holtz, E G.Meyron]] |
| - | [[Category: Shaibi S]] | + | [[Category: Izbicki, B]] |
| - | [[Category: Spektor L]] | + | [[Category: Shaibi, S]] |
| - | [[Category: Zalk R]] | + | [[Category: Spektor, L]] |
| - | [[Category: Zarivach R]] | + | [[Category: Zalk, R]] |
| + | [[Category: Zarivach, R]] | ||
| + | [[Category: Biomineralization]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Nano-reactor]] | ||
| + | [[Category: Radiation damage assisted single-particle analysis]] | ||
Revision as of 07:06, 27 January 2022
Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor
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