2E11

The Crystal Structure of XC1258 from Xanthomonas campestris: A CN-hydrolase Superfamily Protein with an Arsenic Adduct in the Active Site

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.73 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.140 
  • R-Value Observed: 0.186 

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This is version 1.3 of the entry. See complete history. 


Literature

The crystal structure of XC1258 from Xanthomonas campestris: A putative procaryotic Nit protein with an arsenic adduct in the active site

Chin, K.-H., Tsai, Y.-D., Chan, N.-L., Huang, K.-F., Wang, A.H.-J., Chou, S.-H.

(2007) Proteins 69: 665-671


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hydrolase
A, B, C, D
266Xanthomonas campestris pv. campestrisMutation(s): 0 
EC: 3
UniProt
Find proteins for Q8P8M3 (Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25))
Explore Q8P8M3 
Go to UniProtKB:  Q8P8M3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8P8M3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.73 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.140 
  • R-Value Observed: 0.186 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 143.28α = 90
b = 154.305β = 90
c = 51.158γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
ADSCdata collection
DENZOdata reduction
HKL-2000data scaling
SOLVEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-08-07
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.2: 2019-11-06
    Changes: Data collection
  • Version 1.3: 2024-03-13
    Changes: Data collection, Database references, Derived calculations