1cax: Difference between revisions

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<StructureSection load='1cax' size='340' side='right'caption='[[1cax]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1cax' size='340' side='right'caption='[[1cax]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1cax]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Canen Canen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CAX FirstGlance]. <br>
<table><tr><td colspan='2'>[[1cax]] is a 6 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=1CAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CAX FirstGlance]. <br>
</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=1cax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cax OCA], [https://pdbe.org/1cax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cax RCSB], [https://www.ebi.ac.uk/pdbsum/1cax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cax ProSAT]</span></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]] 2.6&#8491;</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=1cax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cax OCA], [https://pdbe.org/1cax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cax RCSB], [https://www.ebi.ac.uk/pdbsum/1cax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cax ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CANA_CANEN CANA_CANEN]] Seed storage protein.  
[https://www.uniprot.org/uniprot/CANA_CANEN CANA_CANEN] Seed storage protein.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=1cax ConSurf].
</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=1cax ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Canavalin, the major reserve protein of the jack bean, was obtained in four different crystal forms. From the structure determined by multiple isomorphous replacement in a hexagonal unit cell, the structures of three other crystals were determined by molecular replacement. In two cases, the rhombohedral and cubic crystals, placement was facilitated by coincidence of threefold molecular symmetry with crystallographic operators. In the orthorhombic crystal the canavalin trimer was the asymmetric unit. The rhombohedral, orthorhombic and cubic crystal structures were subsequently refined using a combination of several approaches with resulting R factors of 0.194, 0.185 and 0.211 at resolutions of 2.6, 2.6 and 2.3 A, respectively. Variation in the conformation of the molecule from crystal to crystal was small with an r.m.s. deviation in Calpha positions of 0.89 A. Packing is quite different among crystal forms but lattice interactions appear to play little role in the conformation of the molecule. Greatest variations in mean position are for those residues that also exhibit the greatest thermal motion. Crystal contacts in all crystals are mediated almost exclusively by hydrophilic side chains, and three to six intermolecular salt bridges per protein subunit are present in each case.
Determination of three crystal structures of canavalin by molecular replacement.,Ko TP, Ng JD, Greenwood A, McPherson A Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):478-89. PMID:15299507<ref>PMID:15299507</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1cax" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Canen]]
[[Category: Canavalia ensiformis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Day, J]]
[[Category: Day J]]
[[Category: Greenwood, A]]
[[Category: Greenwood A]]
[[Category: Ko, T-P]]
[[Category: Ko T-P]]
[[Category: McPherson, A]]
[[Category: McPherson A]]
[[Category: Ng, J D]]
[[Category: Ng JD]]
[[Category: Seed storage protein]]

Latest revision as of 09:42, 7 February 2024

DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENTDETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT

Structural highlights

1cax is a 6 chain structure with sequence from Canavalia ensiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CANA_CANEN Seed storage protein.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1cax, resolution 2.60Å

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OCA
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