1a4f
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a4f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anser_indicus Anser indicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4F FirstGlance]. <br> | <table><tr><td colspan='2'>[[1a4f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anser_indicus Anser indicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4F 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=OXY:OXYGEN+MOLECULE'>OXY</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]] 2Å</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=OXY:OXYGEN+MOLECULE'>OXY</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=1a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4f OCA], [https://pdbe.org/1a4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4f RCSB], [https://www.ebi.ac.uk/pdbsum/1a4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4f 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=1a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4f OCA], [https://pdbe.org/1a4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4f RCSB], [https://www.ebi.ac.uk/pdbsum/1a4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/HBA_ANSIN HBA_ANSIN] 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]] | ||
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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=1a4f 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=1a4f ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | We have determined the crystal structure of bar-headed goose haemoglobin in the oxy form to a resolution of 2.0 A. The R-factor of the model is 19.8%. The structure is similar to human HbA, but contacts between the subunits show slightly altered packing of the tetramer. Bar-headed goose blood shows a greatly elevated oxygen affinity compared to closely related species of geese. This is apparently due to a single proline to alanine mutation at the alpha 1 beta 1 interface which destabilises the T state of the protein. The beta chain N and C termini are well-localized, and together with other neighbouring basic groups they form a strongly positively charged groove at the entrance to the central cavity around the molecular dyad. The well-ordered conformation and the three-dimensional distribution of positive charges clearly indicate this area to be the inositol pentaphosphate binding site of bird haemoglobins. | ||
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- | The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form).,Zhang J, Hua Z, Tame JR, Lu G, Zhang R, Gu X J Mol Biol. 1996 Jan 26;255(3):484-93. PMID:8568892<ref>PMID:8568892</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1a4f" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | *[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Anser indicus]] | [[Category: Anser indicus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Gu | + | [[Category: Gu X]] |
- | [[Category: Zhang | + | [[Category: Zhang J]] |
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Current revision
BAR-HEADED GOOSE HEMOGLOBIN (OXY FORM)
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