1ONA

CO-CRYSTALS OF CONCANAVALIN A WITH METHYL-3,6-DI-O-(ALPHA-D-MANNOPYRANOSYL)-ALPHA-D-MANNOPYRANOSIDE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.221 
  • R-Value Observed: 0.221 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history


Literature

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.

(1996) J Biol Chem 271: 30614-30618

  • DOI: https://doi.org/10.1074/jbc.271.48.30614
  • Primary Citation of Related Structures:  
    1ONA

  • PubMed Abstract: 

    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.


  • Organizational Affiliation

    Laboratorium voor Ultrastruktuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B-1640 Sint-Genesius-Rode, Belgium. bouckaej@vub.ac.be


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CONCANAVALIN A
A, B, C, D
237Canavalia ensiformisMutation(s): 0 
UniProt
Find proteins for P02866 (Canavalia ensiformis)
Explore P02866 
Go to UniProtKB:  P02866
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02866
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

Help

Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]methyl alpha-D-mannopyranoside
E, F, G, H
3N/A
Glycosylation Resources
GlyTouCan:  G27351BJ
GlyCosmos:  G27351BJ
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.221 
  • R-Value Observed: 0.221 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.83α = 90
b = 64.84β = 93.87
c = 125.92γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
MADNESdata reduction
CCP4data scaling
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-09-17
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2016-02-17
    Changes: Derived calculations, Non-polymer description
  • Version 1.4: 2018-04-18
    Changes: Data collection, Other
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Database references, Derived calculations, Structure summary
  • Version 2.1: 2023-08-09
    Changes: Database references, Refinement description, Structure summary