3V6Y

crystal structure of FBF-2 in complex with a mutant gld-1 FBEa13 RNA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.185 
  • R-Value Observed: 0.188 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Divergence of PUF protein specificity through variations in an RNA-binding pocket

Qiu, C.Kershner, A.Wang, Y.Holley, C.H.Wilinski, D.Keles, S.Kimble, J.Wickens, M.Hall, T.M.T.

(2012) J Biol Chem 


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Fem-3 mRNA-binding factor 2413Caenorhabditis elegansMutation(s): 0 
Gene Names: fbf-2F21H12.5
UniProt
Find proteins for Q09312 (Caenorhabditis elegans)
Explore Q09312 
Go to UniProtKB:  Q09312
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ09312
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
RNA (5'-R(*UP*AP*CP*UP*GP*UP*GP*CP*CP*AP*UP*AP*C)-3')13Caenorhabditis elegans
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.185 
  • R-Value Observed: 0.188 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 99.797α = 90
b = 99.797β = 90
c = 105.598γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-01-04
    Type: Initial release