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[[Image:1ymc.jpg|left|200px]]
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{{STRUCTURE_1ymc|  PDB=1ymc  |  SCENE=  }}
'''THREE-DIMENSIONAL STRUCTURE OF CYANOMET-SULFMYOGLOBIN C'''


==THREE-DIMENSIONAL STRUCTURE OF CYANOMET-SULFMYOGLOBIN C==
<StructureSection load='1ymc' size='340' side='right'caption='[[1ymc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ymc]] 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=1YMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YMC 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</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=1ymc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ymc OCA], [https://pdbe.org/1ymc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ymc RCSB], [https://www.ebi.ac.uk/pdbsum/1ymc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ymc ProSAT]</span></td></tr>
</table>
== 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ym/1ymc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ymc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The atomic structure of horse heart cyanomet-sulfmyoglobin C has been established by x-ray crystallographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfmyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sulfur atom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket.


==Overview==
Three-dimensional structure of cyanomet-sulfmyoglobin C.,Evans SV, Sishta BP, Mauk AG, Brayer GD Proc Natl Acad Sci U S A. 1994 May 24;91(11):4723-6. PMID:8197124<ref>PMID:8197124</ref>
The atomic structure of horse heart cyanomet-sulfmyoglobin C has been established by x-ray crystallographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfmyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sulfur atom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1YMC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMC OCA].
</div>
<div class="pdbe-citations 1ymc" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Three-dimensional structure of cyanomet-sulfmyoglobin C., Evans SV, Sishta BP, Mauk AG, Brayer GD, Proc Natl Acad Sci U S A. 1994 May 24;91(11):4723-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8197124 8197124]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brayer, G D.]]
[[Category: Brayer GD]]
[[Category: Evans, S V.]]
[[Category: Evans SV]]
[[Category: Oxygen transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:30:32 2008''

Latest revision as of 07:35, 13 August 2026

THREE-DIMENSIONAL STRUCTURE OF CYANOMET-SULFMYOGLOBIN C

1ymc, resolution 2.00Å

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