5ile: Difference between revisions
Jump to navigation
Jump to search
m Protected "5ile" [edit=sysop:move=sysop] |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==H64A sperm whale myoglobin with a Fe-tolyl moiety== | |||
<StructureSection load='5ile' size='340' side='right'caption='[[5ile]], [[Resolution|resolution]] 1.77Å' scene=''> | |||
== Structural highlights == | |||
<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='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> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
Bioorganometallic 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<ref>PMID:27687333</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Richter-Addo | <div class="pdbe-citations 5ile" style="background-color:#fffaf0;"></div> | ||
[[Category: Thomas | |||
[[Category: Wang | ==See Also== | ||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Physeter catodon]] | |||
[[Category: Richter-Addo GB]] | |||
[[Category: Thomas LM]] | |||
[[Category: Wang B]] | |||
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
|
| ||||||||||||||||||