1XFF

Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Work: 0.161 
  • R-Value Observed: 0.161 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Substrate Binding is Required for Assembly of the Active Conformation of the Catalytic Site in Ntn Amidotransferases: Evidence from the 1.8 Angstrom Crystal Structure of the Glutaminase Domain of Glucosamine 6-Phosphate Synthase

Isupov, M.N.Obmolova, G.Butterworth, S.Badet-Denisot, M.-A.Badet, B.Polikarpov, I.Littlechild, J.A.Teplyakov, A.

(1996) Structure 4: 801-810

  • DOI: https://doi.org/10.1016/s0969-2126(96)00087-1
  • Primary Citation of Related Structures:  
    1XFF, 1XFG

  • PubMed Abstract: 

    Amidotransferases use the amide nitrogen of glutamine in a number of important biosynthetic reactions. They are composed of a glutaminase domain, which catalyzes the hydrolysis of glutamine to glutamate and ammonia, and a synthetase domain, catalyzing amination of the substrate. To gain insight into the mechanism of nitrogen transfer, we examined the structure of the glutaminase domain of glucosamine 6-phosphate synthase (GLMS).


  • Organizational Affiliation

    Department of Chemistry and Biological Sciences, University of Exeter, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glucosamine--fructose-6-phosphate aminotransferase [isomerizing]
A, B
240Escherichia coliMutation(s): 0 
Gene Names: GLMS
EC: 2.6.1.16
UniProt
Find proteins for P17169 (Escherichia coli (strain K12))
Explore P17169 
Go to UniProtKB:  P17169
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP17169
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Work: 0.161 
  • R-Value Observed: 0.161 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 70.38α = 90
b = 82.52β = 90
c = 86.05γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
REFMACrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-09-28
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-10-03
    Changes: Data collection, Database references
  • Version 1.4: 2023-08-23
    Changes: Data collection, Database references, Derived calculations, Refinement description