2REY

Crystal structure of the PDZ domain of human dishevelled 2 (homologous to Drosophila dsh)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.55 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.212 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of the PDZ domains of human dishevelled 2 (homologous to Drosophila dsh).

Papagrigoriou, E.Gileadi, C.Elkins, J.Cooper, C.Ugochukwu, E.Turnbull, A.Pike, A.C.W.Gileadi, O.von Delft, F.Sundstrom, M.Arrowsmith, C.H.Weigelt, J.Edwards, A.M.Doyle, D.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Segment polarity protein dishevelled homolog DVL-2100Homo sapiensMutation(s): 0 
Gene Names: DVL2
UniProt & NIH Common Fund Data Resources
Find proteins for O14641 (Homo sapiens)
Explore O14641 
Go to UniProtKB:  O14641
PHAROS:  O14641
GTEx:  ENSG00000004975 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO14641
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.55 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.212 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.644α = 90
b = 69.644β = 90
c = 57.54γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
MAR345data collection
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2007-10-23
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2017-10-25
    Changes: Refinement description
  • Version 1.3: 2023-08-30
    Changes: Data collection, Database references, Refinement description