3e1q: Difference between revisions

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==Crystal structure of W133F variant E. coli Bacterioferritn with iron.==
==Crystal structure of W133F variant E. coli Bacterioferritn with iron.==
<StructureSection load='3e1q' size='340' side='right' caption='[[3e1q]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3e1q' size='340' side='right'caption='[[3e1q]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3e1q]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E1Q FirstGlance]. <br>
<table><tr><td colspan='2'>[[3e1q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1Q FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e1j|3e1j]], [[3e1l|3e1l]], [[3e1m|3e1m]], [[3e1n|3e1n]], [[3e1o|3e1o]], [[3e1p|3e1p]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e1j|3e1j]], [[3e1l|3e1l]], [[3e1m|3e1m]], [[3e1n|3e1n]], [[3e1o|3e1o]], [[3e1p|3e1p]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BFR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3e1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1q OCA], [http://pdbe.org/3e1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e1q RCSB], [http://www.ebi.ac.uk/pdbsum/3e1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1q ProSAT]</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=3e1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1q OCA], [https://pdbe.org/3e1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e1q RCSB], [https://www.ebi.ac.uk/pdbsum/3e1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BFR_ECOLI BFR_ECOLI]] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.<ref>PMID:10769150</ref> <ref>PMID:14636073</ref>   
[[https://www.uniprot.org/uniprot/BFR_ECOLI BFR_ECOLI]] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.<ref>PMID:10769150</ref> <ref>PMID:14636073</ref>   
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Ferritin|Ferritin]]
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Brun, N E.Le]]
[[Category: Brun, N E.Le]]
[[Category: Crow, A]]
[[Category: Crow, A]]
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