1PKY

PYRUVATE KINASE FROM E. COLI IN THE T-STATE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.305 
  • R-Value Observed: 0.203 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition.

Mattevi, A.Valentini, G.Rizzi, M.Speranza, M.L.Bolognesi, M.Coda, A.

(1995) Structure 3: 729-741

  • DOI: https://doi.org/10.1016/s0969-2126(01)00207-6
  • Primary Citation of Related Structures:  
    1PKY

  • PubMed Abstract: 

    Pyruvate kinase (PK) plays a major role in the regulation of glycolysis. Its catalytic activity is controlled by the substrate phosphoenolpyruvate and by one or more allosteric effectors. The crystal structures of the non-allosteric PKs from cat and rabbit muscle are known. We have determined the three-dimensional structure of the allosteric type I PK from Escherichia coli, in order to study the mechanism of allosteric regulation.


  • Organizational Affiliation

    Department of Genetics and Microbiology, University of Pavia, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PYRUVATE KINASE
A, B, C, D
470Escherichia coliMutation(s): 0 
EC: 2.7.1.40
UniProt
Find proteins for P0AD61 (Escherichia coli (strain K12))
Explore P0AD61 
Go to UniProtKB:  P0AD61
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AD61
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.305 
  • R-Value Observed: 0.203 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.911α = 90
b = 129.577β = 90
c = 241.37γ = 90
Software Package:
Software NamePurpose
PROLSQrefinement
DENZOdata reduction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

  • Released Date: 1995-12-07 
  • Deposition Author(s): Mattevi, A.

Revision History  (Full details and data files)

  • Version 1.0: 1995-12-07
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Other