4BQK

rice importin_alpha : VirD2NLS complex

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.224 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.197 

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history. 


Literature

Structural Basis of Interaction of Bipartite Nuclear Localization Signal from Agrobacterium Vird2 with Rice Importin-Alpha

Chang, C.-W., Williams, S.J., Counago, R.M., Kobe, B.

(2014) Mol Plant 7: 1061

  • DOI: https://doi.org/10.1093/mp/ssu014
  • Primary Citation of Related Structures:  
    4BPL, 4BQK
    • Organizational Affiliation: 

    School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, Qld 4072, Australia.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
IMPORTIN SUBUNIT ALPHA-1A
A, B
456Oryza sativaMutation(s): 0 
UniProt
Find proteins for Q71VM4 (Oryza sativa subsp. japonica)
Explore Q71VM4 
Go to UniProtKB:  Q71VM4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ71VM4
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
T-DNA BORDER ENDONUCLEASE VIRD2
C, D
20Agrobacterium tumefaciensMutation(s): 0 
EC: 3.1
UniProt
Find proteins for P18592 (Agrobacterium fabrum (strain C58 / ATCC 33970))
Explore P18592 
Go to UniProtKB:  P18592
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP18592
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.224 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.197 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 62.803α = 90
b = 140.948β = 90
c = 72.632γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
SCALAdata scaling
MOLREPphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-02-19
    Type: Initial release
  • Version 1.1: 2014-06-18
    Changes: Database references
  • Version 2.0: 2023-12-20
    Changes: Atomic model, Data collection, Database references, Derived calculations, Other, Refinement description