3shx
From Proteopedia
(Difference between revisions)
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==Frog M-ferritin with magnesium, L134P mutant== | ==Frog M-ferritin with magnesium, L134P mutant== | ||
<StructureSection load='3shx' size='340' side='right' caption='[[3shx]], [[Resolution|resolution]] 1.35Å' scene=''> | <StructureSection load='3shx' size='340' side='right' caption='[[3shx]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3shx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3shx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/American_bullfrog American bullfrog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SHX 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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3se1|3se1]], [[3sh6|3sh6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3se1|3se1]], [[3sh6|3sh6]]</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='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=3shx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3shx RCSB], [http://www.ebi.ac.uk/pdbsum/3shx PDBsum]</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=3shx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shx OCA], [http://pdbe.org/3shx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3shx RCSB], [http://www.ebi.ac.uk/pdbsum/3shx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3shx ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/FRI2_LITCT FRI2_LITCT]] 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. |
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: American bullfrog]] | ||
[[Category: Ferroxidase]] | [[Category: Ferroxidase]] | ||
- | [[Category: Rana catesbeiana]] | ||
[[Category: Alber, T]] | [[Category: Alber, T]] | ||
[[Category: Ng, H L]] | [[Category: Ng, H L]] |
Revision as of 14:35, 5 August 2016
Frog M-ferritin with magnesium, L134P mutant
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Categories: American bullfrog | Ferroxidase | Alber, T | Ng, H L | Theil, E C | Tosha, T | Diiron | Iron storage | Metal-binding | Oxidoreductase