1ona
From Proteopedia
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|PDB= 1ona |SIZE=350|CAPTION= <scene name='initialview01'>1ona</scene>, resolution 2.35Å | |PDB= 1ona |SIZE=350|CAPTION= <scene name='initialview01'>1ona</scene>, resolution 2.35Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1ona FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ona OCA], [http://www.ebi.ac.uk/pdbsum/1ona PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ona RCSB]</span> | ||
}} | }} | ||
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[[Category: Poortmans, F.]] | [[Category: Poortmans, F.]] | ||
[[Category: Wyns, L.]] | [[Category: Wyns, L.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MN]] | ||
[[Category: calcium]] | [[Category: calcium]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| Line 35: | Line 36: | ||
[[Category: signal]] | [[Category: signal]] | ||
| - | ''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 22:47:42 2008'' |
Revision as of 19:47, 30 March 2008
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| , resolution 2.35Å | |||||||
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| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CO-CRYSTALS OF CONCANAVALIN A WITH METHYL-3,6-DI-O-(ALPHA-D-MANNOPYRANOSYL)-ALPHA-D-MANNOPYRANOSIDE
Overview
The structure of concanavalin A in complex with the trimannoside methyl-3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside has been determined in a novel space group. In three of the four subunits of the concanavalin A tetramer, the interactions between the protein and the bound saccharide are essentially identical to those reported previously by other authors (Naismith, J. H., and Field, R. A. (1996) J. Biol. Chem. 271, 972-976). In the fourth subunit, however, the alpha1-->3 linkage has a different conformation, resulting in a different part of the alpha1-->3-linked mannose interacting with essentially the same surface of the protein. Furthermore, significant differences are observed in the quaternary associations of the subunits compared with the saccharide-free structures and other carbohydrate complexes, suggesting that the concanavalin A tetramer is a rather flexible entity.
About this Structure
1ONA is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
Reference
A structure of the complex between concanavalin A and methyl-3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside reveals two binding modes., Loris R, Maes D, Poortmans F, Wyns L, Bouckaert J, J Biol Chem. 1996 Nov 29;271(48):30614-8. PMID:8940035
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