4fwy: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "4fwy" [edit=sysop:move=sysop] |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==F33Y CuB myoglobin (F33Y L29H F43H sperm whale myoglobin) with copper bound== | ||
<StructureSection load='4fwy' size='340' side='right'caption='[[4fwy]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fwy]] 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=4FWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FWY 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <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=4fwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fwy OCA], [https://pdbe.org/4fwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fwy RCSB], [https://www.ebi.ac.uk/pdbsum/4fwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fwy 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4fwy" 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]] | |||
Latest revision as of 10:58, 13 August 2026
F33Y CuB myoglobin (F33Y L29H F43H sperm whale myoglobin) with copper bound
| ||||||||||||
