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==ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE== | ==ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE== | ||
<StructureSection load='1bz6' size='340' side='right' caption='[[1bz6]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='1bz6' size='340' side='right' caption='[[1bz6]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
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<table><tr><td colspan='2'>[[1bz6]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BZ6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1bz6]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BZ6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bz6 OCA], [http://pdbe.org/1bz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bz6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bz6 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bz6 OCA], [http://pdbe.org/1bz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bz6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bz6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1bz6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1bz6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:48, 8 November 2017
ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATUREATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE
Structural highlights
Function[MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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