View source for 1gkb


==CONCANAVALIN A, NEW CRYSTAL FORM==
<StructureSection load='1gkb' size='340' side='right'caption='[[1gkb]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gkb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1e0i 1e0i]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GKB 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]] 1.56&#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=MG:MAGNESIUM+ION'>MG</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=1gkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gkb OCA], [https://pdbe.org/1gkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gkb RCSB], [https://www.ebi.ac.uk/pdbsum/1gkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gkb 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/gk/1gkb_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=1gkb ConSurf].
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== Publication Abstract from PubMed ==
A structure of native concanavalin A (ConA), a hardy perennial of structural biology, has been determined in a dimeric crystal form at a resolution of 1.56 A (space group C222(1); unit-cell parameters a = 118.70, b = 101.38, c = 111.97 A; two molecules in the asymmetric unit). The structure has been refined to an R(free) of 0.206 (R = 0.178) after iterative model building and phase-bias removal using Shake&amp;wARP. Correspondence between calculated water-tyrosine interactions and experimentally observed structures near the saccharide-binding site suggests that the observed interactions between Tyr12 and water in various crystal forms are to be expected and are not unique to the presence of an active site. The present structure differs from previously reported atomic resolution structures of ConA in several regions and extends insight into the conformational flexibility of this molecule. Furthermore, this third, low-temperature, structure of ConA in a different crystal form, independently refined using powerful model-bias removal techniques, affords the opportunity to revisit assessment of accuracy and precision in high- or atomic resolution protein structures. It is illustrated that several precise structures of the same molecule can differ substantially in local detail and users of crystallographic models are reminded to consider the potential impact when interpreting structures. Suggestions on how to effectively represent ensembles of crystallographic models of a given molecule are provided.

Concanavalin A in a dimeric crystal form: revisiting structural accuracy and molecular flexibility.,Kantardjieff KA, Hochtl P, Segelke BW, Tao FM, Rupp B Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):735-43. Epub 2002, Apr 26. PMID:11976483<ref>PMID:11976483</ref>

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

==See Also==
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Canavalia ensiformis]]
[[Category: Large Structures]]
[[Category: Hoechtl P]]
[[Category: Kantardjieff K]]
[[Category: Rupp B]]
[[Category: Segelke B]]