1USH

5'-NUCLEOTIDASE FROM E. COLI

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.73 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.180 
  • R-Value Observed: 0.180 

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This is version 1.4 of the entry. See complete history. 


Literature

X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site.

Knofel, T., Strater, N.

(1999) Nat Struct Biol 6: 448-453

  • DOI: https://doi.org/10.1038/8253
  • Primary Citation of Related Structures:  
    1USH, 2USH

  • PubMed Abstract: 

    The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system.

    • Organizational Affiliation: 

    Institut für Kristallographie, Abteilung Saenger, Freie Universität Berlin, Germany.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
5'-NUCLEOTIDASE550Escherichia coli K-12Mutation(s): 0 
Gene Names: USHA
EC: 3.1.3.5
UniProt
Find proteins for P07024 (Escherichia coli (strain K12))
Explore P07024 
Go to UniProtKB:  P07024
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07024
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.73 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.180 
  • R-Value Observed: 0.180 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 83.61α = 90
b = 83.61β = 90
c = 181.63γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
X-PLORrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-06-15
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2011-11-16
    Changes: Atomic model
  • Version 1.4: 2024-04-03
    Changes: Data collection, Database references, Derived calculations, Refinement description