3GK6

Crystal structure from the mobile metagenome of Vibrio cholerae. Integron cassette protein VCH_CASS2.

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.185 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history. 


Literature

Crystal Structure of an Integron Gene Cassette-Associated Protein from Vibrio cholerae Identifies a Cationic Drug-Binding Module.

Deshpande, C.N., Harrop, S.J., Boucher, Y., Hassan, K.A., Leo, R.D., Xu, X., Cui, H., Savchenko, A., Chang, C., Labbate, M., Paulsen, I.T., Stokes, H.W., Curmi, P.M., Mabbutt, B.C.

(2011) PLoS One 6: e16934-e16934

  • DOI: https://doi.org/10.1371/journal.pone.0016934
  • Primary Citation of Related Structures:  
    3GK6

  • PubMed Abstract: 

    The direct isolation of integron gene cassettes from cultivated and environmental microbial sources allows an assessment of the impact of the integron/gene cassette system on the emergence of new phenotypes, such as drug resistance or virulence. A structural approach is being exploited to investigate the modularity and function of novel integron gene cassettes.

    • Organizational Affiliation: 

    Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, New South Wales, Australia.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Integron cassette protein VCH_CASS2170Vibrio choleraeMutation(s): 0 
Gene Names: OPVCH_OP4G
UniProt
Find proteins for D0VX23 (Vibrio cholerae)
Explore D0VX23 
Go to UniProtKB:  D0VX23
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupD0VX23
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PE4
Query on PE4
Download Ideal Coordinates CCD File 
B [auth A]2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
C16 H34 O8
PJWQOENWHPEPKI-UHFFFAOYSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.185 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.378α = 90
b = 59.378β = 90
c = 95.756γ = 120
Software Package:
Software NamePurpose
ADSCdata collection
AutoSolphasing
PHENIXrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-03-24
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance