1hqw: Difference between revisions

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OCA

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 ==CRYSTAL STRUCTURE OF THE COMPLEX OF CONCANAVALIN A WITH A TRIPEPTIDE YPY==
-<StructureSection load='1hqw' size='340' side='right' caption='[[1hqw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='1hqw' size='340' side='right'caption='[[1hqw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hqw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HQW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hqw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HQW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PTD:PENTANEDIAL'>PTD</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]] 2.4&#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=1hqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqw OCA], [http://pdbe.org/1hqw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hqw RCSB], [http://www.ebi.ac.uk/pdbsum/1hqw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hqw ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PTD:PENTANEDIAL'>PTD</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=1hqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqw OCA], [https://pdbe.org/1hqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hqw RCSB], [https://www.ebi.ac.uk/pdbsum/1hqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hqw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CONA_CANCT CONA_CANCT]] Glucose/D-mannose specific lectin.
+[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/1hqw_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/1hqw_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 19: / Line 20: @@
 </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=1hqw ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The X-ray structure analysis of a cross-linked crystal of concanavalin A soaked with the tripeptide molecule as the probe molecule showed electron density corresponding to full occupation in the binding pocket. The site lies on the surface of concanavalin A and is surrounded by three symmetry-related molecules. The crystal structure of the tripeptide complex was refined at 2.4-A resolution to an R-factor of 17.5%, (Rfree factor of 23.7%), with an RMS deviation in bond distances of 0.01 A. The model includes all 237 residue of concanavalin A, 1 manganese ion, 1 calcium ion, 161 water molecules, 1 glutaraldehyde molecule, and 1 tripeptide molecule. This X-ray structure analysis also provides an approach to mapping the binding surface of crystalline protein with a probe molecule that is dissolved in a mixture of organic solvent with water or in neat organic solvent but is hardly dissolved in aqueous solution.
-Crystal structure of the complex of concanavalin A and tripeptide.,Zhang Z, Qian M, Huang Q, Jia Y, Tang Y, Wang K, Cui D, Li M J Protein Chem. 2001 Jan;20(1):59-65. PMID:11330349<ref>PMID:11330349</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1hqw" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Concanavalin A|Concanavalin A]]
+*[[Concanavalin 3D structures|Concanavalin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Canavalia ensiformis]]
-[[Category: Cui, D]]
+[[Category: Large Structures]]
-[[Category: Huang, Q]]
+[[Category: Cui D]]
-[[Category: Jia, Y]]
+[[Category: Huang Q]]
-[[Category: Li, M]]
+[[Category: Jia Y]]
-[[Category: Qian, M]]
+[[Category: Li M]]
-[[Category: Tang, Y]]
+[[Category: Qian M]]
-[[Category: Wang, K]]
+[[Category: Tang Y]]
-[[Category: Zhang, Z]]
+[[Category: Wang K]]
-[[Category: Beta sheet]]
+[[Category: Zhang Z]]
-[[Category: Lectin binding]]