1a4f: Difference between revisions
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<table><tr><td colspan='2'>[[1a4f]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A4F FirstGlance]. <br> | <table><tr><td colspan='2'>[[1a4f]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A4F 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=OXY:OXYGEN+MOLECULE'>OXY</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=OXY:OXYGEN+MOLECULE'>OXY</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=1a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a4f RCSB], [http://www.ebi.ac.uk/pdbsum/1a4f 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=1a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4f OCA], [http://pdbe.org/1a4f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a4f RCSB], [http://www.ebi.ac.uk/pdbsum/1a4f PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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 1a4f" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 18:58, 9 September 2015
BAR-HEADED GOOSE HEMOGLOBIN (OXY FORM)BAR-HEADED GOOSE HEMOGLOBIN (OXY FORM)
Structural highlights
Function[HBA_ANSIN] Involved in oxygen transport from the lung to the various peripheral tissues. [HBB_ANSIN] 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 PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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