5ile: Difference between revisions
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==H64A sperm whale myoglobin with a Fe-tolyl moiety== | ==H64A sperm whale myoglobin with a Fe-tolyl moiety== | ||
<StructureSection load='5ile' size='340' side='right' caption='[[5ile]], [[Resolution|resolution]] 1.77Å' scene=''> | <StructureSection load='5ile' size='340' side='right'caption='[[5ile]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ile]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ile]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ILE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ILE FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6CQ:[3,3-(7,12-DIETHENYL-3,8,13,17-TETRAMETHYLPORPHYRIN-2,18-DIYL-KAPPA~4~N~21~,N~22~,N~23~,N~24~)DI(PROPANOATO)(2-)](3-METHYLPHENYL)IRON'>6CQ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6CQ:[3,3-(7,12-DIETHENYL-3,8,13,17-TETRAMETHYLPORPHYRIN-2,18-DIYL-KAPPA~4~N~21~,N~22~,N~23~,N~24~)DI(PROPANOATO)(2-)](3-METHYLPHENYL)IRON'>6CQ</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=5ile FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ile OCA], [https://pdbe.org/5ile PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ile RCSB], [https://www.ebi.ac.uk/pdbsum/5ile PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ile ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5ile" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ile" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Physeter catodon]] | ||
[[Category: | [[Category: Richter-Addo GB]] | ||
[[Category: Thomas LM]] | |||
[[Category: Wang B]] | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 17:00, 30 August 2023
H64A sperm whale myoglobin with a Fe-tolyl moietyH64A sperm whale myoglobin with a Fe-tolyl moiety
Structural highlights
FunctionMYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Publication Abstract from PubMedBioorganometallic Fe-C bonds are biologically relevant species that may result from the metabolism of natural or synthetic hydrazines. The molecular structures of four new sperm whale mutant myoglobin derivatives with Fe-aryl moieties, namely H64A-tolyl-m, H64A-chlorophenyl-p, H64Q-tolyl-m, and H64Q-chlorophenyl-p, have been determined at 1.7-1.9A resolution. The structures reveal conformational preferences for the substituted aryls resulting from attachment of the aryl ligands to Fe at the site of net -NHNH2 release from the precursor hydrazines, and show distal pocket changes that readily accommodate these bulky ligands. Organometallic myoglobins: Formation of Fe-carbon bonds and distal pocket effects on aryl ligand conformations.,Wang B, Thomas LM, Richter-Addo GB J Inorg Biochem. 2016 Jun 24. pii: S0162-0134(16)30192-1. doi:, 10.1016/j.jinorgbio.2016.06.028. PMID:27687333[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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