1NUH

The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.51 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.217 

Starting Model: experimental
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This is version 1.4 of the entry. See complete history. 


Literature

The structure of human phosphoglucose isomerase complexed with a transition-state analogue.

Davies, C., Muirhead, H., Chirgwin, J.

(2003) Acta Crystallogr D Biol Crystallogr 59: 1111-1113

  • DOI: https://doi.org/10.1107/s0907444903007352
  • Primary Citation of Related Structures:  
    1NUH

  • PubMed Abstract: 

    Phosphoglucose isomerase (PGI) is a workhorse enzyme of carbohydrate metabolism that interconverts glucose 6-phosphate and fructose 6-phosphate. Outside the cell, however, the protein appears to function as a cytokine. A crystal structure of human PGI bound with 5-phosphoarabinonate, a strong inhibitor that mimics the cis-enediol(ate) intermediate of the reaction, has been determined at 2.5 A resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction.

    • Organizational Affiliation: 

    Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA. [email protected]


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
glucose phosphate isomerase558Homo sapiensMutation(s): 0 
Gene Names: GPI
EC: 5.3.1.9
UniProt & NIH Common Fund Data Resources
Find proteins for P06744 (Homo sapiens)
Explore P06744 
Go to UniProtKB:  P06744
PHAROS:  P06744
GTEx:  ENSG00000105220 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06744
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.51 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.217 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 94.4α = 90
b = 94.4β = 90
c = 137.1γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
CrystalCleardata reduction
CrystalCleardata scaling

Structure Validation

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Entry History 

Deposition Data

  • Released Date: 2003-02-11 
    • Deposition Author(s): Davies, C.

Revision History  (Full details and data files)

  • Version 1.0: 2003-02-11
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2018-01-24
    Changes: Database references
  • Version 1.4: 2023-08-16
    Changes: Data collection, Database references, Derived calculations, Refinement description