1CD5

GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.207 

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This is version 1.3 of the entry. See complete history. 


Literature

The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution.

Horjales, E., Altamirano, M.M., Calcagno, M.L., Garratt, R.C., Oliva, G.

(1999) Structure 7: 527-537

  • DOI: https://doi.org/10.1016/s0969-2126(99)80069-0
  • Primary Citation of Related Structures:  
    1CD5

  • PubMed Abstract: 

    The allosteric hexameric enzyme glucosamine-6-phosphate deaminase from Escherichia coli catalyses the regulatory step of N-acetylglucosamine catabolism, which consists of the isomerisation and deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonia. The reversibility of the catalysis and its rapid-equilibrium random kinetic mechanism, among other properties, make this enzyme a good model for studying allosteric processes.

    • Organizational Affiliation: 

    Instituto de Biotecnología, Universidad Nacional Autónoma de México (UNAM), Cuernavaca, Mor, Mexico. horjales@ibt.unam.mx


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (GLUCOSAMINE 6-PHOSPHATE DEAMINASE)266Escherichia coli K-12Mutation(s): 0 
UniProt
Find proteins for P0A759 (Escherichia coli (strain K12))
Explore P0A759 
Go to UniProtKB:  P0A759
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A759
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.252 
  • R-Value Work: 0.207 
  • Space Group: P 63 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 129.81α = 90
b = 129.81β = 90
c = 139.11γ = 120
Software Package:
Software NamePurpose
AMoREphasing
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
CCP4data scaling
SCALAdata scaling
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-03-06
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2023-08-09
    Changes: Data collection, Database references, Refinement description