3WCY

Murine Ifnar1 in complex with interferon-beta

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.286 
  • R-Value Work: 0.237 
  • R-Value Observed: 0.239 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history. 


Literature

Structural basis of a unique interferon beta signaling axis mediated via the IFNAR1 receptor

de Weerd, N.A., Vivian, J.P., Nguyen, T.K., Mangan, N.E., Gould, J.A., Braniff, S.J., Zaker-Tabrizi, L., Fung, K.Y., Forster, S.C., Beddoe, T., Reid, H.H., Rossjohn, J., Hertzog, P.J.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Interferon alpha/beta receptor 1403Mus musculusMutation(s): 0 
Gene Names: Ifar, Ifnar, Ifnar1
UniProt & NIH Common Fund Data Resources
Find proteins for P33896 (Mus musculus)
Explore P33896 
Go to UniProtKB:  P33896
IMPC:  MGI:107658
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP33896
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Interferon betaB [auth I]161Mus musculusMutation(s): 0 
Gene Names: Ifb, Ifnb, Ifnb1
UniProt
Find proteins for P01575 (Mus musculus)
Explore P01575 
Go to UniProtKB:  P01575
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01575
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.286 
  • R-Value Work: 0.237 
  • R-Value Observed: 0.239 
  • Space Group: P 43
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.591α = 90
b = 54.591β = 90
c = 239.801γ = 90
Software Package:
Software NamePurpose
Blu-Icedata collection
PHASERphasing
BUSTERrefinement
MOSFLMdata reduction
SCALAdata scaling

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: 2013-07-24
    Type: Initial release
  • Version 1.1: 2023-11-08
    Changes: Data collection, Database references, Refinement description