1OUN

CRYSTAL STRUCTURE OF NUCLEAR TRANSPORT FACTOR 2 (NTF2)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.158 

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This is version 1.5 of the entry. See complete history


Literature

The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2).

Bullock, T.L.Clarkson, W.D.Kent, H.M.Stewart, M.

(1996) J Mol Biol 260: 422-431

  • DOI: https://doi.org/10.1006/jmbi.1996.0411
  • Primary Citation of Related Structures:  
    1OUN

  • PubMed Abstract: 

    Nuclear transport factor 2 (NTF2) facilitates protein transport into the nucleus and interacts with both the small Ras-like GTPase Ran and nucleoporin p62. We have determined the structure of bacterially expressed rat NTF2 at 1.6 angstroms resolution using X-ray crystallography. The NTF2 polypeptide chain forms an alpha + beta barrel that opens at one end to form a distinctive hydrophobic cavity and its fold is homologous to that of scytalone dehydratase. The NTF2 hydrophobic cavity is a candidate for a potential binding site for other proteins involved in nuclear import such as Ran and nucleoporin p62. In addition, the hydrophobic cavity contains a putative catalytic Asp-His pair, which raises the possibility of an unanticipated enzymatic activity of the molecule that may have implications for the molecular mechanism of nuclear protein import.


  • Organizational Affiliation

    MRC Laboratory of Molecular Biology, Cambridge, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEAR TRANSPORT FACTOR 2
A, B
127Rattus norvegicusMutation(s): 0 
UniProt
Find proteins for P61972 (Rattus norvegicus)
Explore P61972 
Go to UniProtKB:  P61972
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP61972
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.158 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 56α = 90
b = 58.1β = 90
c = 88.3γ = 90
Software Package:
Software NamePurpose
TNTrefinement
SHELXrefinement
SHELXmodel building
MOSFLMdata reduction
CCP4data scaling
SHELXphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-04-01
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-07-17
    Changes: Advisory, Data collection, Other, Refinement description
  • Version 1.4: 2019-08-14
    Changes: Data collection
  • Version 1.5: 2024-02-14
    Changes: Advisory, Data collection, Database references