2F4E

N-terminal domain of FKBP42 from Arabidopsis thaliana

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.32 Å
  • R-Value Free: 0.283 
  • R-Value Work: 0.246 
  • R-Value Observed: 0.248 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters.

Weiergraber, O.H., Eckhoff, A., Granzin, J.

(2006) FEBS Lett 580: 251-255

  • DOI: https://doi.org/10.1016/j.febslet.2005.12.007
  • Primary Citation of Related Structures:  
    2F4E

  • PubMed Abstract: 

    We present the three-dimensional structure of the N-terminal FK506-binding protein (FKBP)-like domain of the immunophilin FKBP42 from Arabidopsis thaliana. The data provide the structural background for the explanation of key functional properties reported previously.

    • Organizational Affiliation: 

    Institut für Biologische Informationsverarbeitung, IBI-2, Biologische Strukturforschung, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
AtFKBP42
A, B
180Arabidopsis thalianaMutation(s): 0 
Gene Names: TWD1
UniProt
Find proteins for Q9LDC0 (Arabidopsis thaliana)
Explore Q9LDC0 
Go to UniProtKB:  Q9LDC0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9LDC0
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.32 Å
  • R-Value Free: 0.283 
  • R-Value Work: 0.246 
  • R-Value Observed: 0.248 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 34.98α = 90
b = 62.767β = 90
c = 122.778γ = 90
Software Package:
Software NamePurpose
SCALAdata scaling
CNSrefinement
PDB_EXTRACTdata extraction
MOSFLMdata reduction
CCP4data scaling
TRUNCATEdata scaling
MOLREPphasing

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: 2006-01-10
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description
  • Version 1.4: 2023-08-23
    Changes: Data collection, Database references, Refinement description