1y8h: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1y8h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y8H FirstGlance]. <br> | <table><tr><td colspan='2'>[[1y8h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y8H FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> | ||
<tr id=' | <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=1y8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y8h OCA], [https://pdbe.org/1y8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y8h RCSB], [https://www.ebi.ac.uk/pdbsum/1y8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y8h 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=1y8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y8h OCA], [https://pdbe.org/1y8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y8h RCSB], [https://www.ebi.ac.uk/pdbsum/1y8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y8h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE] 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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[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Biswal | [[Category: Biswal BK]] | ||
[[Category: Sankaranarayanan | [[Category: Sankaranarayanan R]] | ||
[[Category: Vijayan | [[Category: Vijayan M]] | ||
Latest revision as of 09:53, 23 August 2023
HORSE METHEMOGLOBIN LOW SALT, PH 7.0HORSE METHEMOGLOBIN LOW SALT, PH 7.0
Structural highlights
FunctionHBA_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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