4fwx: Difference between revisions

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New page: '''Unreleased structure''' The entry 4fwx is ON HOLD Authors: Gao, Y.-G., Stoner-Ma, D., Robinson, H., Petrik, I.D., Miner, K.D., Lu, Y. Description: Aquoferric F33Y CuB myoglobin (F33...
 
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'''Unreleased structure'''


The entry 4fwx is ON HOLD
==Aquoferric F33Y CuB myoglobin (F33Y L29H F43H sperm whale myoglobin)==
<StructureSection load='4fwx' size='340' side='right'caption='[[4fwx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4fwx]] 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=4FWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FWX 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=4fwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fwx OCA], [https://pdbe.org/4fwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fwx RCSB], [https://www.ebi.ac.uk/pdbsum/4fwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fwx 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 ==
No spare Tyr: Rational design of functional enzymes with a high number of turnovers is a challenge, especially those with a complex active site, such as respiratory oxidases. Introducing two His and one Tyr residues into myoglobin resulted in enzymes that reduce O(2) to H(2) O with more than 1000 turnovers (red line, see scheme) and minimal release of reactive oxygen species. The positioning of the Tyr residue is critical for activity.


Authors: Gao, Y.-G., Stoner-Ma, D., Robinson, H., Petrik, I.D., Miner, K.D., Lu, Y.
A Designed Functional Metalloenzyme that Reduces O(2) to H(2) O with Over One Thousand Turnovers.,Miner KD, Mukherjee A, Gao YG, Null EL, Petrik ID, Zhao X, Yeung N, Robinson H, Lu Y Angew Chem Int Ed Engl. 2012 Jun 4;51(23):5589-92. doi: 10.1002/anie.201201981., Epub 2012 Apr 26. PMID:22539151<ref>PMID:22539151</ref>


Description: Aquoferric F33Y CuB myoglobin (F33Y L29H F43H sperm whale myoglobin)
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4fwx" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Gao Y-G]]
[[Category: Lu Y]]
[[Category: Miner KD]]
[[Category: Petrik ID]]
[[Category: Robinson H]]
[[Category: Stoner-Ma D]]
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