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1qdc
From Proteopedia
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|PDB= 1qdc |SIZE=350|CAPTION= <scene name='initialview01'>1qdc</scene>, resolution 2.0Å | |PDB= 1qdc |SIZE=350|CAPTION= <scene name='initialview01'>1qdc</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qdc OCA], [http://www.ebi.ac.uk/pdbsum/1qdc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qdc RCSB]</span> | ||
}} | }} | ||
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[[Category: Loris, R.]] | [[Category: Loris, R.]] | ||
[[Category: Wyns, L.]] | [[Category: Wyns, L.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MN]] | ||
[[Category: carbohydrate binding]] | [[Category: carbohydrate binding]] | ||
[[Category: concanavalin some]] | [[Category: concanavalin some]] | ||
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[[Category: plant lectin]] | [[Category: plant lectin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:12 2008'' |
Revision as of 20:12, 30 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MAN(APLHA1-6)MAN(ALPHA1-O)METHYL CONCANAVALIN A COMPLEX
Overview
The crystal structures of concanavalin A in complex with Man(alpha1-6)Man(alpha1-O)Me and Man(alpha1-3)Man(alpha1-O)Me were determined at resolutions of 2.0 and 2.8 A, respectively. In both structures, the O-1-linked mannose binds in the conserved monosaccharide-binding site. The O-3-linked mannose of Man(alpha1-3)Man(alpha1-O)Me binds in the hydrophobic subsite formed by Tyr-12, Tyr-100, and Leu-99. The shielding of a hydrophobic surface is consistent with the associated large heat capacity change. The O-6-linked mannose of Man(alpha1-6)Man(alpha1-O)Me binds in the same subsite formed by Tyr-12 and Asp-16 as the reducing mannose of the highly specific trimannose Man(alpha1-3)[Man(alpha1-6)]Man(alpha1-O)Me. However, it is much less tightly bound. Its O-2 hydroxyl makes no hydrogen bond with the conserved water 1. Water 1 is present in all the sugar-containing concanavalin A structures and increases the complementarity between the protein-binding surface and the sugar, but is not necessarily a hydrogen-bonding partner. A water analysis of the carbohydrate-binding site revealed a conserved water molecule replacing O-4 on the alpha1-3-linked arm of the trimannose. No such water is found for the reducing or O-6-linked mannose. Our data indicate that the central mannose of Man(alpha1-3)[Man(alpha1-6)]Man(alpha1-O)Me primarily functions as a hinge between the two outer subsites.
About this Structure
1QDC is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
Reference
The crystal structures of Man(alpha1-3)Man(alpha1-O)Me and Man(alpha1-6)Man(alpha1-O)Me in complex with concanavalin A., Bouckaert J, Hamelryck TW, Wyns L, Loris R, J Biol Chem. 1999 Oct 8;274(41):29188-95. PMID:10506175
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