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6v7l

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'''Unreleased structure'''
 
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The entry 6v7l is ON HOLD
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==The structure of the P212121 crystal form of canavalin at 173 K==
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<StructureSection load='6v7l' size='340' side='right'caption='[[6v7l]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6v7l]] is a 3 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=6V7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V7L FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6v7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v7l OCA], [https://pdbe.org/6v7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v7l RCSB], [https://www.ebi.ac.uk/pdbsum/6v7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v7l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CANA_CANEN CANA_CANEN] Seed storage protein.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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X-ray intensities extending to 1.4 A resolution were collected on the P63 hexagonal crystal form of canavalin, and extended to 1.9 A for the orthorhombic C2221 crystals. Structure determination of a new crystal form of canavalin having space group P212121 is reported as well. Both the N and C terminal cupin domains contained identifiable ligands. For hexagonal crystals, in the cavity of the C terminal cupin, a molecule of benzoic acid was found, bound through carboxyl oxygens to Histidine 297, asparagine 284 and Arginine 376. The benzene ring was immersed in a cluster of at least 8 hydrophobic amino acid side chains. The N terminal cupin contained a molecule of citrate. Benzoic acid was also found to be present in the C terminal cupins of in the C2221 and P212121 crystal forms. In rhombohedral crystals, the C terminal cupin domain appeared to be occupied by a phosphate ion, but this was ambiguous. In cubic crystals, both domains were vacant. The N terminal cupin domains of canavalin in the P212121 and rhombohedral crystals were also vacant, but the N terminal cupin domain of the C2221 crystals contained a ligand whose identity is uncertain, but which has been modeled as HEPES buffer. A possible physiological role for the ligands and their complexes with canavalin is considered.
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Authors: McPherson, A.
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Binding of benzoic acid and anions within the cupin domains of the vicilin protein canavalin from jack bean (Canavalia ensiformis): Crystal structures.,McPherson A Biochem Biophys Res Commun. 2020 Jan 23. pii: S0006-291X(20)30176-5. doi:, 10.1016/j.bbrc.2020.01.101. PMID:31983433<ref>PMID:31983433</ref>
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Description: The structure of the P212121 crystal form of canavalin at 173 K
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Mcpherson, A]]
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<div class="pdbe-citations 6v7l" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Canavalia ensiformis]]
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[[Category: Large Structures]]
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[[Category: McPherson A]]

Current revision

The structure of the P212121 crystal form of canavalin at 173 K

PDB ID 6v7l

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