2VWR

Crystal structure of the second pdz domain of numb-binding protein 2


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.30 Å
  • R-Value Free: 0.177 
  • R-Value Work: 0.134 
  • R-Value Observed: 0.136 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal Structure of the Second Pdz Domain of the Human Numb-Binding Protein 2

Roos, A.K.Guo, K.Burgess-Brown, N.Yue, W.W.Elkins, J.M.Pike, A.C.W.Filippakopoulos, P.Arrowsmith, C.H.Wikstom, M.Edwards, A.von Delft, F.Bountra, C.Doyle, D.Oppermann, U.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
LIGAND OF NUMB PROTEIN X 295Homo sapiensMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for Q8N448 (Homo sapiens)
Explore Q8N448 
Go to UniProtKB:  Q8N448
PHAROS:  Q8N448
GTEx:  ENSG00000139517 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8N448
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.30 Å
  • R-Value Free: 0.177 
  • R-Value Work: 0.134 
  • R-Value Observed: 0.136 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.773α = 90
b = 38.643β = 117.22
c = 38.186γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2008-09-16
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-24
    Changes: Database references, Structure summary
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description