2F8M

Ribose 5-phosphate isomerase from Plasmodium falciparum


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.09 Å
  • R-Value Free: 0.272 
  • R-Value Work: 0.208 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure of ribose 5-phosphate isomerase from Plasmodium falciparum.

Holmes, M.A.Buckner, F.S.Van Voorhis, W.C.Verlinde, C.L.Mehlin, C.Boni, E.DeTitta, G.Luft, J.Lauricella, A.Anderson, L.Kalyuzhniy, O.Zucker, F.Schoenfeld, L.W.Earnest, T.N.Hol, W.G.Merritt, E.A.

(2006) Acta Crystallogr Sect F Struct Biol Cryst Commun 62: 427-431

  • DOI: https://doi.org/10.1107/S1744309106010876
  • Primary Citation of Related Structures:  
    2F8M

  • PubMed Abstract: 

    The structure of ribose 5-phosphate isomerase from Plasmodium falciparum, PFE0730c, has been determined by molecular replacement at 2.09 angstroms resolution. The enzyme, which catalyzes the isomerization reaction that interconverts ribose 5-phosphate and ribulose 5-phosphate, is a member of the pentose phosphate pathway. The P. falciparum enzyme belongs to the ribose 5-phosphate isomerase A family, Pfam family PF06562 (DUF1124), and is structurally similar to other members of the family.


  • Organizational Affiliation

    Structural Genomics of Pathogenic Protozoa (SGPP) Consortium, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ribose 5-phosphate isomerase
A, B
244Plasmodium falciparum 3D7Mutation(s): 0 
Gene Names: PFE0730c
EC: 5.3.1.6
UniProt
Find proteins for Q8I3W2 (Plasmodium falciparum (isolate 3D7))
Explore Q8I3W2 
Go to UniProtKB:  Q8I3W2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8I3W2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.09 Å
  • R-Value Free: 0.272 
  • R-Value Work: 0.208 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 93.689α = 90
b = 136.23β = 90
c = 45.011γ = 90
Software Package:
Software NamePurpose
EPMRphasing
PDB_EXTRACTdata extraction
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-12-27
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description
  • Version 1.4: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description