1y8h: Difference between revisions
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</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jy7|1jy7]], [[1lfq|1lfq]], [[1y8i|1y8i]], [[1y8k|1y8k]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jy7|1jy7]], [[1lfq|1lfq]], [[1y8i|1y8i]], [[1y8k|1y8k]]</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=1y8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y8h RCSB], [http://www.ebi.ac.uk/pdbsum/1y8h 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=1y8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y8h OCA], [http://pdbe.org/1y8h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y8h RCSB], [http://www.ebi.ac.uk/pdbsum/1y8h 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 1y8h" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 04:35, 12 September 2015
HORSE METHEMOGLOBIN LOW SALT, PH 7.0HORSE METHEMOGLOBIN LOW SALT, PH 7.0
Structural highlights
Function[HBA_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues. [HBB_HORSE] 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 PubMedA new relaxed state has been characterized in the crystals of horse methemoglobin grown at neutral pH at low ionic concentration and their low humidity variants. The crystals provide an example for improvement in X-ray diffraction quality with reduced solvent content. Only the classical R state has been so far observed in liganded horse hemoglobin. The state characterized in the present study lies in between the R state and the R2 state characterized earlier in liganded human hemoglobin. The results presented here, along with those of earlier studies, suggest that relaxed and tense hemoglobin can access ensembles of states. A new relaxed state in horse methemoglobin characterized by crystallographic studies.,Sankaranarayanan R, Biswal BK, Vijayan M Proteins. 2005 Aug 15;60(3):547-51. PMID:15887226[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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