1bz6: Difference between revisions

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-[[Image:1bz6.gif|left|200px]]
- {{Structure
+==ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE==
-|PDB= 1bz6 |SIZE=350|CAPTION= <scene name='initialview01'>1bz6</scene>, resolution 1.2&Aring;
+<StructureSection load='1bz6' size='340' side='right'caption='[[1bz6]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
+<table><tr><td colspan='2'>[[1bz6]] 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=1BZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BZ6 FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
-|GENE=
+<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'>[https://proteopedia.org/fgij/fg.htm?mol=1bz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bz6 OCA], [https://pdbe.org/1bz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bz6 RCSB], [https://www.ebi.ac.uk/pdbsum/1bz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bz6 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.
+== 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/bz/1bz6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1bz6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structures of myoglobin in the deoxy- and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide.
-'''ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE'''
+A steric mechanism for inhibition of CO binding to heme proteins.,Kachalova GS, Popov AN, Bartunik HD Science. 1999 Apr 16;284(5413):473-6. PMID:10205052<ref>PMID:10205052</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1bz6" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The crystal structures of myoglobin in the deoxy- and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide.
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-BZ6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BZ6 OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-A steric mechanism for inhibition of CO binding to heme proteins., Kachalova GS, Popov AN, Bartunik HD, Science. 1999 Apr 16;284(5413):473-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10205052 10205052]
 [[Category: Physeter catodon]]
-[[Category: Single protein]]
+[[Category: Bartunik HD]]
-[[Category: Bartunik, H D.]]
+[[Category: Kachalova GS]]
-[[Category: Kachalova, G S.]]
+[[Category: Popov AN]]
-[[Category: Popov, A N.]]
-[[Category: HEM]]
-[[Category: SO4]]
-[[Category: atomic resolution]]
-[[Category: heme]]
-[[Category: oxygen transport]]
-[[Category: respiratory protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:17:46 2008''