1nxd: Difference between revisions
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==Crystal structure of MnMn Concanavalin A== | ==Crystal structure of MnMn Concanavalin A== | ||
<StructureSection load='1nxd' size='340' side='right' caption='[[1nxd]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1nxd' size='340' side='right'caption='[[1nxd]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1nxd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Canen Canen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NXD FirstGlance]. <br> | <table><tr><td colspan='2'>[[1nxd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Canen Canen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NXD FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nx/1nxd_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nx/1nxd_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1nxd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1nxd" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Concanavalin 3D structures|Concanavalin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Canen]] | [[Category: Canen]] | ||
[[Category: Large Structures]] | |||
[[Category: Albert, A]] | [[Category: Albert, A]] | ||
[[Category: Gonzalez-Ramirez, L A]] | [[Category: Gonzalez-Ramirez, L A]] | ||
Revision as of 10:43, 21 August 2019
Structural highlights
Function[CONA_CANEN] D-mannose specific lectin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedConcanavalin A has been crystallized in the presence of the ligand (6-S-beta-D-galactopyranosyl-6-thio)-cyclomaltoheptaose. The crystals are isomorphous to those reported for ConA complexed with peptides at low resolution (3.00-2.75 angstroms). The structure was solved at 1.9 angstroms, with free R and R values of 0.201 and 0.184, respectively. As expected, no molecules of the ligand were bound to the protein. Soaking in the cryobuffer left its fingerprint as 25 molecules of glycerol in the bound solvent, most of them at specific positions. The fact that a glycerol molecule is located in the sugar-binding pocket of each of the four subunits in the asymmetric unit and another is located in two of the peptide-binding sites suggests a recognition phenomenon rather than a displacement of water molecules by glycerol. Crystal contact analysis shows that a relation exists between the residues that form hydrogen bonds to other asymmetric units and the space group: contact Asp58-Ser62 is a universal feature of ConA crystals, while Ser66-His121, Asn69-Asn118 and Tyr100-His205 contacts are general features of the C222(1) crystal form. Structure of concanavalin A at pH 8: bound solvent and crystal contacts.,Lopez-Jaramillo FJ, Gonzalez-Ramirez LA, Albert A, Santoyo-Gonzalez F, Vargas-Berenguel A, Otalora F Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1048-56. Epub 2004, May 21. PMID:15159564[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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