1qpw: Difference between revisions

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 <StructureSection load='1qpw' size='340' side='right'caption='[[1qpw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qpw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QPW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qpw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QPW 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1qpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpw OCA], [http://pdbe.org/1qpw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qpw RCSB], [http://www.ebi.ac.uk/pdbsum/1qpw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qpw ProSAT]</span></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=1qpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpw OCA], [https://pdbe.org/1qpw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qpw RCSB], [https://www.ebi.ac.uk/pdbsum/1qpw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qpw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HBA_PIG HBA_PIG]] Involved in oxygen transport from the lung to the various peripheral tissues. [[http://www.uniprot.org/uniprot/HBB_PIG HBB_PIG]] Involved in oxygen transport from the lung to the various peripheral tissues.
+[https://www.uniprot.org/uniprot/HBA_PIG HBA_PIG] Involved in oxygen transport from the lung to the various peripheral tissues.
 == Evolutionary Conservation ==
 [[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=1qpw ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-To investigate a potential candidate material for making artificial red blood cells to supplement blood transfusion, the X-ray structure of porcine haemoglobin at 1.8 A resolution was determined as part of research towards synthesizing human blood. Porcine haemoglobin was crystallized by the vapor-diffusion method, producing crystals of dimensions 0.3-0.5 mm after successive seeding. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 68.10, b = 72.27, c = 114.85 A. The initial phase was determined by the molecular-replacement method, using human oxyhaemoglobin as a model. The final R factor was 21.1% for 36 820 reflections after validation of 574 water molecules. The r.m.s. deviations of bond lengths, angles, torsion angles and improper angles from their ideal values are 0.017 A, 3.0, 20.6 and 1.8 degrees, respectively. The average B factor is 33.63 A(2) for the haemoglobin molecule and 50.53 A(2) for the water molecules. The structure could be superimposed on a 2.8 A resolution structure with an r.m.s. difference of 0.59 A in main-chain atomic positions and 1. 27 A in side-chain atomic positions. Porcine and human haemoglobins are compared. A tentative model for artificial blood is proposed based on the complementarity relationship of the surface charges between haemoglobin and the surrounding cell membrane.
-Structure determination of porcine haemoglobin.,Lu TH, Panneerselvam K, Liaw YC, Kan P, Lee CJ Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):304-12. PMID:10713517<ref>PMID:10713517</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1qpw" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
 [[Category: Sus scrofa]]
-[[Category: Kan, P]]
+[[Category: Kan P]]
-[[Category: Lee, C J]]
+[[Category: Lee C-J]]
-[[Category: Liaw, Y C]]
+[[Category: Liaw Y-C]]
-[[Category: Lu, T H]]
+[[Category: Lu T-H]]
-[[Category: Panneerselvam, K]]
+[[Category: Panneerselvam K]]
-[[Category: Artificial human blood]]
-[[Category: Oxygen transport]]
-[[Category: Porcine hemoglobin]]
-[[Category: X-ray study]]