6PFK

PHOSPHOFRUCTOKINASE, INHIBITED T-STATE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.188 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Structural basis of the allosteric behaviour of phosphofructokinase.

Schirmer, T.Evans, P.R.

(1990) Nature 343: 140-145

  • DOI: https://doi.org/10.1038/343140a0
  • Primary Citation of Related Structures:  
    6PFK

  • PubMed Abstract: 

    Comparison between the crystal structures of low- and high-affinity forms of phosphofructokinase shows a close coupling between the change of quaternary structure and local changes triggered by binding of the allosteric effectors. These concerted changes link all the substrate and effector sites in the tetramer, and explain the change of affinity for the cooperative substrate.


  • Organizational Affiliation

    MRC Laboratory of Molecular Biology, Cambridge, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PHOSPHOFRUCTOKINASE
A, B, C, D
319Geobacillus stearothermophilusMutation(s): 0 
Gene Names: PFK
EC: 2.7.1.11
UniProt
Find proteins for P00512 (Geobacillus stearothermophilus)
Explore P00512 
Go to UniProtKB:  P00512
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00512
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.188 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 132α = 90
b = 115.2β = 90
c = 96.2γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-07-11
    Type: Initial release
  • Version 1.1: 2008-03-25
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2011-08-10
    Changes: Other
  • Version 1.4: 2024-03-13
    Changes: Data collection, Database references, Derived calculations, Other