3ZYT

Structure Determination of EstA from Arthrobacter nitroguajacolicus Rue61a


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.181 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal Structure Analysis of Esta from Arthrobacter Sp. Rue61A--an Insight Into Catalytic Promiscuity.

Wagner, U.G.Dimaio, F.Kolkenbrock, S.Fetzner, S.

(2014) FEBS Lett 588: 1154

  • DOI: https://doi.org/10.1016/j.febslet.2014.02.045
  • Primary Citation of Related Structures:  
    3ZYT

  • PubMed Abstract: 

    In this article we analyze the reasons for catalytic promiscuity of a type VIII esterase with β-lactamase fold and the ability to cleave β-lactams. We compared the structure of this enzyme to those of an esterase of the same type without any lactamase ability, an esterase with moderate lactamase ability, and a class C β-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven.


  • Organizational Affiliation

    Institute of Molecular Biosciences, University of Graz, A-8010 Graz, Austria. Electronic address: ulrike.wagner@uni-graz.at.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ESTERASE A372Paenarthrobacter nitroguajacolicusMutation(s): 0 
UniProt
Find proteins for K4DIE4 (Paenarthrobacter nitroguajacolicus)
Explore K4DIE4 
Go to UniProtKB:  K4DIE4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupK4DIE4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.181 
  • Space Group: I 41 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 191.246α = 90
b = 191.246β = 90
c = 191.246γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
SCALAdata scaling
PHENIX-ROSETTAphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-09-19
    Type: Initial release
  • Version 1.1: 2014-10-22
    Changes: Database references
  • Version 1.2: 2019-07-17
    Changes: Data collection