1EWY

ANABAENA PCC7119 FERREDOXIN:FERREDOXIN-NADP+-REDUCTASE COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.38 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.232 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule.

Morales, R.Kachalova, G.Vellieux, F.Charon, M.H.Frey, M.

(2000) Acta Crystallogr D Biol Crystallogr 56: 1408-1412

  • DOI: https://doi.org/10.1107/s0907444900010052
  • Primary Citation of Related Structures:  
    1EWY

  • PubMed Abstract: 

    Ferredoxin-NADP(+) reductase (FNR) and its physiological electron donor ferredoxin (Fd) from the cyanobacterium Anabaena PCC7119 have been co-crystallized. The unit-cell parameters are a = b = 63.72, c = 158.02 A and the space group is P2(1)2(1)2(1). The crystal structure has been solved with 2.4 A resolution synchrotron data by molecular replacement, anomalous dispersion and R(min) search methods. For the computations, the crystal was treated as a merohedral twin. The asymmetric unit contains two FNR molecules and one ferredoxin molecule. The packing of the FNR molecules displays a nearly tetragonal symmetry (space group P4(3)2(1)2), whereas the ferredoxin arrangement is orthorhombic. This study provides the first crystallographic model of a dissociable complex between FNR and Fd.


  • Organizational Affiliation

    LCCP, Institut de Biologie Structurale J. P. Ebel, CEA-CNRS, 41 Rue Jules Horowitz, F38027 Grenoble, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FERREDOXIN-NADP REDUCTASE
A, B
303Nostoc sp. PCC 7119Mutation(s): 0 
EC: 1.18.1.2
UniProt
Find proteins for P21890 (Nostoc sp. (strain ATCC 29151 / PCC 7119))
Explore P21890 
Go to UniProtKB:  P21890
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP21890
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
FERREDOXIN I98Nostoc sp. PCC 7119Mutation(s): 0 
UniProt
Find proteins for P0A3C8 (Nostoc sp. (strain ATCC 29151 / PCC 7119))
Explore P0A3C8 
Go to UniProtKB:  P0A3C8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A3C8
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.38 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.232 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.73α = 90
b = 63.72β = 90
c = 158.02γ = 90
Software Package:
Software NamePurpose
AMoREphasing
SHELXL-97refinement
MOSFLMdata reduction
CCP4data scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-02-07
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-09
    Changes: Data collection, Database references, Derived calculations, Refinement description