2BPI

Structure of Iron dependent superoxide dismutase from P. falciparum.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.52 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.187 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

The Crystal Structure of Superoxide Dismutase from Plasmodium Falciparum.

Boucher, I.W.Brzozowski, A.M.Brannigan, J.A.Schnick, C.Smith, D.J.Kyes, S.A.Wilkinson, A.J.

(2006) BMC Struct Biol 6: 20

  • DOI: https://doi.org/10.1186/1472-6807-6-20
  • Primary Citation of Related Structures:  
    2BPI

  • PubMed Abstract: 

    Superoxide dismutases (SODs) are important enzymes in defence against oxidative stress. In Plasmodium falciparum, they may be expected to have special significance since part of the parasite life cycle is spent in red blood cells where the formation of reactive oxygen species is likely to be promoted by the products of haemoglobin breakdown. Thus, inhibitors of P. falciparum SODs have potential as anti-malarial compounds. As a step towards their development we have determined the crystal structure of the parasite's cytosolic iron superoxide dismutase.


  • Organizational Affiliation

    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, UK. boucher@ysbl.york.ac.uk


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FE-SUPEROXIDE DISMUTASE
A, B
206Plasmodium falciparum 3D7Mutation(s): 0 
EC: 1.15.1.1
UniProt
Find proteins for Q8IAY6 (Plasmodium falciparum (isolate 3D7))
Explore Q8IAY6 
Go to UniProtKB:  Q8IAY6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8IAY6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.52 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.187 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 55.941α = 90
b = 78.91β = 90
c = 90.621γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-10-11
    Type: Initial release
  • Version 1.1: 2013-04-24
    Changes: Derived calculations, Non-polymer description, Other, Structure summary, Version format compliance
  • Version 1.2: 2015-04-15
    Changes: Structure summary
  • Version 1.3: 2020-03-04
    Changes: Advisory, Derived calculations, Other
  • Version 1.4: 2023-12-13
    Changes: Advisory, Data collection, Database references, Derived calculations, Refinement description