4BRZ

Haloalkane dehalogenase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.67 Å
  • R-Value Free: 0.246 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.207 

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This is version 1.1 of the entry. See complete history


Literature

Biochemical and Structural Characterisation of a Haloalkane Dehalogenase from a Marine Rhodobacteraceae.

Novak, H.R.Sayer, C.Isupov, M.N.Gotz, D.Spragg, A.M.Littlechild, J.A.

(2014) FEBS Lett 588: 1616

  • DOI: https://doi.org/10.1016/j.febslet.2014.02.056
  • Primary Citation of Related Structures:  
    4BRZ, 4C6H

  • PubMed Abstract: 

    A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity. A deeper substrate binding pocket defines the enzyme preference towards substrates with longer carbon chains. Arg136 at the bottom of the substrate pocket is positioned to bind the distal halogen group of extended di-halogenated substrates.


  • Organizational Affiliation

    The Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HALOALKANE DEHALOGENASE
A, B
290ParacoccaceaeMutation(s): 0 
UniProt
Find proteins for A0A067XG63 (Paracoccaceae)
Explore A0A067XG63 
Go to UniProtKB:  A0A067XG63
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A067XG63
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.67 Å
  • R-Value Free: 0.246 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.207 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.97α = 90
b = 75.52β = 92.94
c = 64.87γ = 90
Software Package:
Software NamePurpose
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-05-14
    Type: Initial release
  • Version 1.1: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description