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==CRYSTAL STRUCTURE OF AQUOMET HEMOGLOBIN-I OF THE MANED WOLF (CHRYSOCYON BRACHYURUS) AT 2.0 RESOLUTION.== | ==CRYSTAL STRUCTURE OF AQUOMET HEMOGLOBIN-I OF THE MANED WOLF (CHRYSOCYON BRACHYURUS) AT 2.0 RESOLUTION.== | ||
<StructureSection load='1fhj' size='340' side='right' caption='[[1fhj]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1fhj' size='340' side='right'caption='[[1fhj]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fhj]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1fhj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chrysocyon_brachyurus Chrysocyon brachyurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FHJ 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></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]] 1.8Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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></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=1fhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhj OCA], [https://pdbe.org/1fhj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fhj RCSB], [https://www.ebi.ac.uk/pdbsum/1fhj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fhj ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HBA_CHRBR HBA_CHRBR] Involved in oxygen transport from the lung to the various peripheral tissues. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/1fhj_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/1fhj_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1fhj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 24: | Line 28: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1fhj" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 32: | Line 37: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Chrysocyon brachyurus]] | [[Category: Chrysocyon brachyurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Fadel | [[Category: Fadel V]] | ||
[[Category: | [[Category: De Azevedo WF]] | ||
Latest revision as of 09:03, 9 August 2023
CRYSTAL STRUCTURE OF AQUOMET HEMOGLOBIN-I OF THE MANED WOLF (CHRYSOCYON BRACHYURUS) AT 2.0 RESOLUTION.CRYSTAL STRUCTURE OF AQUOMET HEMOGLOBIN-I OF THE MANED WOLF (CHRYSOCYON BRACHYURUS) AT 2.0 RESOLUTION.
Structural highlights
FunctionHBA_CHRBR Involved in oxygen transport from the lung to the various peripheral tissues. 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 PubMedCrystal structure of hemoglobin isolated from the Brazilian maned wolf (Chrysocyon brachyurus) was determined using standard molecular replacement technique and refined using maximum-likelihood and simulated annealing protocols to 1.87A resolution. Structural and functional comparisons between hemoglobins from the Chrysocyon brachyurus and Homo sapiens are discussed, in order to provide further insights in the comparative biochemistry of vertebrate hemoglobins. Crystal structure of hemoglobin from the maned wolf (Chrysocyon brachyurus) using synchrotron radiation.,Fadel V, Canduri F, Olivieri JR, Smarra AL, Colombo MF, Bonilla-Rodriguez GO, de Azevedo WF Jr Protein Pept Lett. 2003 Dec;10(6):551-9. PMID:14683506[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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