1fcs: Difference between revisions

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<StructureSection load='1fcs' size='340' side='right'caption='[[1fcs]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1fcs' size='340' side='right'caption='[[1fcs]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fcs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1FCS FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fcs]] 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=1FCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FCS FirstGlance]. <br>
</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYNTHETIC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 PHYCD])</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>, <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'>[http://proteopedia.org/fgij/fg.htm?mol=1fcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fcs OCA], [http://pdbe.org/1fcs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fcs RCSB], [http://www.ebi.ac.uk/pdbsum/1fcs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fcs ProSAT]</span></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=1fcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fcs OCA], [https://pdbe.org/1fcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fcs RCSB], [https://www.ebi.ac.uk/pdbsum/1fcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fcs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.  
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1fcs ConSurf].
</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=1fcs ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of sperm whale myoglobin His64(E7)--&gt;Val,Thr67(E10)--&gt;Arg double mutant has been studied by X-ray crystallography at 1.6 A resolution, and refined to a crystallographic R-factor of 0.197. The Arg67(E10) side chain is extended in the direction of the ligand binding site, and its NH1 atom is at a distance of 3.11 A from the NH1 atom of Arg45(CD3), which is also pointing towards the distal site. Both are kept in this position by hydrogen bonding and electrostatic interactions with a solvent sulfate ion, located amongst the two, on the protein surface. No liganded water molecule is present at the sixth coordination position of the Fe(III) heme.
Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution.,Rizzi M, Bolognesi M, Coda A, Cutruzzola F, Allocatelli CT, Brancaccio A, Brunori M FEBS Lett. 1993 Mar 29;320(1):13-6. PMID:8462669<ref>PMID:8462669</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fcs" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phycd]]
[[Category: Physeter catodon]]
[[Category: Allocatelli, C Travaglini]]
[[Category: Bolognesi M]]
[[Category: Bolognesi, M]]
[[Category: Brancaccio A]]
[[Category: Brancaccio, A]]
[[Category: Brunori M]]
[[Category: Brunori, M]]
[[Category: Coda A]]
[[Category: Coda, A]]
[[Category: Cutruzzola F]]
[[Category: Cutruzzola, F]]
[[Category: Rizzi M]]
[[Category: Rizzi, M]]
[[Category: Travaglini Allocatelli C]]
[[Category: Oxygen transport]]