3IXR

Crystal Structure of Xylella fastidiosa PrxQ C47S Mutant


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.198 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Biochemical and Structural Analysis Indicates that PrxQ, a Cys Based Peroxidase from Xylella fastidiosa, possesses high reactivity towards hydroperoxides

Horta, B.B.Oliveira, M.A.Discola, K.F.Cussiol, J.R.R.Netto, L.E.S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Bacterioferritin comigratory protein179Xylella fastidiosaMutation(s): 1 
Gene Names: Peroxiredoxin QXF_0961
EC: 1.11.1.15
UniProt
Find proteins for Q9PER7 (Xylella fastidiosa (strain 9a5c))
Explore Q9PER7 
Go to UniProtKB:  Q9PER7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9PER7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.198 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.973α = 90
b = 39.743β = 90
c = 99.836γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
PHASERphasing
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-03-23
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2021-10-13
    Changes: Database references
  • Version 1.3: 2023-09-06
    Changes: Data collection, Refinement description