1A7U

CHLOROPEROXIDASE T


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.176 
  • R-Value Work: 0.152 
  • R-Value Observed: 0.149 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural investigation of the cofactor-free chloroperoxidases.

Hofmann, B.Tolzer, S.Pelletier, I.Altenbuchner, J.van Pee, K.H.Hecht, H.J.

(1998) J Mol Biol 279: 889-900

  • DOI: https://doi.org/10.1006/jmbi.1998.1802
  • Primary Citation of Related Structures:  
    1A7U, 1A88, 1A8Q, 1A8S, 1A8U, 1BRT

  • PubMed Abstract: 

    The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites.


  • Organizational Affiliation

    Department SF, GBF (Gesellschaft für Biotechnologische Forschung), Mascheroder Weg 1, Braunschweig, D-38124, FRG.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CHLOROPEROXIDASE T
A, B
277Kitasatospora aureofaciensMutation(s): 0 
Gene Names: CPOT
EC: 1.11.1.10
UniProt
Find proteins for O31168 (Kitasatospora aureofaciens)
Explore O31168 
Go to UniProtKB:  O31168
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO31168
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.176 
  • R-Value Work: 0.152 
  • R-Value Observed: 0.149 
  • Space Group: P 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 126.56α = 90
b = 126.56β = 90
c = 126.56γ = 90
Software Package:
Software NamePurpose
CCP4model building
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
CCP4phasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-06-17
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-02
    Changes: Database references, Other, Refinement description