3d4x: Difference between revisions
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<StructureSection load='3d4x' size='340' side='right'caption='[[3d4x]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='3d4x' size='340' side='right'caption='[[3d4x]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3d4x]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3d4x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Felis_catus Felis catus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D4X 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]] 2.2Å</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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d4x OCA], [https://pdbe.org/3d4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d4x RCSB], [https://www.ebi.ac.uk/pdbsum/3d4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d4x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HBA_FELCA HBA_FELCA] 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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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d4/3d4x_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d4/3d4x_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Haemoglobin is a tetrameric protein that plays a vital role in the transport of oxygen from the lungs to the tissues and of carbon dioxide back to the lungs. Even though a large amount of work has already been performed in this area, the study of the haemoglobin structures of avian and mammalian species is rather incomplete. Efforts are being made to understand the salient features of the species mentioned above. Here, whole blood plasma was collected from sheep and goat and purified by anion-exchange chromatography; the haemoglobins were crystallized by the hanging-drop vapour-diffusion method under unbuffered low-salt conditions using PEG 3350 as a precipitant. Data collection was carried out using a MAR345 image-plate detector system. Sheep haemoglobin crystallizes in the orthorhombic space group P2(1)2(1)2(1) with one whole biological molecule (alpha2beta2) in the asymmetric unit, with unit-cell parameters a = 60.231, b = 70.695, c = 131.479 A. In contrast, goat haemoglobin crystallizes in the triclinic system with two biological molecules (alpha2beta2) in the unit cell. The unit-cell parameters are a = 53.103, b = 69.382, c = 96.098 A, alpha = 110.867, beta = 91.133, gamma = 109.437 degrees. | |||
Crystallization of sheep (Ovis aries) and goat (Capra hircus) haemoglobins under unbuffered low-salt conditions.,Neelagandan K, Moorthy PS, Balasubramanian M, Ponnuswamy MN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):887-9. Epub 2007 Sep 19. PMID:017909297<ref>PMID:017909297</ref> | |||
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> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Felis | [[Category: Felis catus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Balasubramanian | [[Category: Balasubramanian M]] | ||
[[Category: Neelagandan K]] | |||
[[Category: Neelagandan | [[Category: Ponnuswamy MN]] | ||
[[Category: Ponnuswamy | [[Category: Sathya Moorthy P]] | ||
[[Category: | |||
Latest revision as of 09:04, 13 August 2026
Crystal structure determination of cat (Felis silvestris catus) hemoglobin at 2.2 angstrom resolution
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