2DH1

Crystal structure of peanut lectin lactose-azobenzene-4,4'-dicarboxylic acid-lactose complex

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 7.65 Å
  • R-Value Free: 0.377 
  • R-Value Work: 0.355 
  • R-Value Observed: 0.356 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Multivalency in lectins - A crystallographic, modelling and light-scattering study involving peanut lectin and a bivalent ligand

Natchiar, S.K., Srinivas, O., Nivedita, M., Sagarika, D., Jayaraman, N., Surolia, A., Vijayan, M.

(2006) Curr Sci 90: 1230-1237


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Galactose-binding lectin
A, B, C, D
236Arachis hypogaeaMutation(s): 0 
UniProt
Find proteins for P02872 (Arachis hypogaea)
Explore P02872 
Go to UniProtKB:  P02872
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02872
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 7.65 Å
  • R-Value Free: 0.377 
  • R-Value Work: 0.355 
  • R-Value Observed: 0.356 
  • Space Group: I 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 92.75α = 90
b = 92.75β = 90
c = 473.5γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
REFMACrefinement

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-08-15
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-10-25
    Changes: Data collection, Database references, Refinement description