1M3I | pdb_00001m3i

Perfringolysin O, new crystal form

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 
    0.280 (Depositor) 
  • R-Value Work: 
    0.233 (Depositor) 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


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


Literature

Structural Snapshots in the Molecular Mechanism of PFO Revealed

Rossjohn, J., Parker, M., Polekhina, G., Feil, S., Tweten, R.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
perfringolysin O
A, B, C, D
471Clostridium perfringensMutation(s): 0 
Gene Names: pfoa
Membrane Entity: Yes 
UniProt
Find proteins for P0C2E9 (Clostridium perfringens (strain 13 / Type A))
Explore P0C2E9 
Go to UniProtKB:  P0C2E9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0C2E9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free:  0.280 (Depositor) 
  • R-Value Work:  0.233 (Depositor) 
Space Group: P 31
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 130.41α = 90
b = 130.41β = 90
c = 129.9γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNSrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-02-03
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Refinement description