View source for 1jbc


==CONCANAVALIN A==
<StructureSection load='1jbc' size='340' side='right'caption='[[1jbc]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jbc]] is a 1 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=1JBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JBC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</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></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=1jbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jbc OCA], [https://pdbe.org/1jbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jbc RCSB], [https://www.ebi.ac.uk/pdbsum/1jbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jbc ProSAT]</span></td></tr>
</table>
== Function ==
[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/jb/1jbc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1jbc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of native concanavalin A has been refined to a resolution of 1.2 A against data collected at 120 K. The space group is I222, with a = 61.954 (8), b = 86.053 (11), c = 89.079 (11) A. The structure was refined by restrained weighted least-squares minimization of sum w(F(o)(2) - F(c)(2)(2) with SHELXL92/3/6. The final model contains all of the atoms from 237 amino acids, two metal ions and 271 water molecules spread over 287 sites. Disorder is modelled over two conformations for 30 amino-acid side chains. The final weighted R index on F(2) (wR(2)) on all data was 30.4%. Conventional R indices based on F were 14.2 and 11.8% for all data and for data with F &gt; 4sigma(F), respectively.

Atomic resolution structure of concanavalin A at 120 K.,Parkin S, Rupp B, Hope H Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1161-8. PMID:15299577<ref>PMID:15299577</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jbc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Canavalia ensiformis]]
[[Category: Large Structures]]
[[Category: Hope H]]
[[Category: Parkin S]]
[[Category: Rupp B]]