1SHK

THE THREE-DIMENSIONAL STRUCTURE OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.222 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.174 

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This is version 1.2 of the entry. See complete history


Literature

Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi.

Krell, T.Coyle, J.E.Horsburgh, M.J.Coggins, J.R.Lapthorn, A.J.

(1997) Acta Crystallogr D Biol Crystallogr 53: 612-614

  • DOI: https://doi.org/10.1107/S0907444997004319
  • Primary Citation of Related Structures:  
    1SHK, 2SHK

  • PubMed Abstract: 

    Shikimate kinase from Erwinia chrysanthemi, overexpressed in Escherichia coli has been crystallized by the vapour-diffusion method using sodium chloride as a precipitant. Mass spectrometry was used to confirm the purity of the shikimate kinase and dynamic light scattering was used to assess conditions for the monodispersity of the enzyme. The crystals are tetragonal, space group P4(1)2(1)2 or enantiomorph with cell dimensions a = b = 108.5 and c = 92.8 A (at 100 K). Native crystals diffract to better than 2.6 A on a synchrotron X-ray source. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 3.6 A(3) Da(-1).


  • Organizational Affiliation

    Division of Biochemistry and Molecular Biology, Institute of Biological and Life Sciences, University of Glasgow, Scotland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SHIKIMATE KINASE
A, B
173Dickeya chrysanthemiMutation(s): 0 
Gene Names: AROL
EC: 2.7.1.71
UniProt
Find proteins for P10880 (Dickeya chrysanthemi)
Explore P10880 
Go to UniProtKB:  P10880
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP10880
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.222 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.174 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 108.5α = 90
b = 108.5β = 90
c = 92.8γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHELX-90model building
SHELX-90refinement
SHELX-90phasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-11-18
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance