3wft: Difference between revisions
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<table><tr><td colspan='2'>[[3wft]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WFT FirstGlance]. <br> | <table><tr><td colspan='2'>[[3wft]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WFT FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3wft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wft OCA], [https://pdbe.org/3wft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wft RCSB], [https://www.ebi.ac.uk/pdbsum/3wft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wft 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=3wft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wft OCA], [https://pdbe.org/3wft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wft RCSB], [https://www.ebi.ac.uk/pdbsum/3wft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wft ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | [https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A conjugate between apomyoglobin and cobalt tetradehydrocorrin was prepared to replicate the coordination behavior of cob(I)alamin in methionine synthase. X-ray crystallography reveals that the tetra-coordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket. | |||
Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model.,Hayashi T, Morita Y, Mizohata E, Oohora K, Ohbayashi J, Inoue T, Hisaeda Y Chem Commun (Camb). 2014 Oct 25;50(83):12560-3. doi: 10.1039/c4cc05448b. PMID:25197974<ref>PMID:25197974</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3wft" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | *[[Myoglobin 3D structures|Myoglobin 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||