1S96

The 2.0 A X-ray structure of Guanylate Kinase from E.coli


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.195 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The Structure of Guanylate Kinase from Escherichia coli at 2.0 A resolution

Kreusch, A.Spraggon, G.Klock, H.E.McMullan, D.Vincent, J.Rodrigues, K.Lesley, S.A.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Guanylate kinase
A, B
219Escherichia coliMutation(s): 6 
Gene Names: GMKSPORB3648C4473SF3688S4081
EC: 2.7.4.8
UniProt
Find proteins for P60546 (Escherichia coli (strain K12))
Explore P60546 
Go to UniProtKB:  P60546
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP60546
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.195 
  • Space Group: P 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 124.552α = 90
b = 124.552β = 90
c = 124.552γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing
CNSrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-02-10
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance