4JRM

Crystal structure of beta-ketoacyl-ACP synthase II (FabF) from Vibrio Cholerae (space group P212121) at 1.75 Angstrom


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.231 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.203 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of beta-ketoacyl-ACP synthase II (FabF) from Vibrio cholerae (space group P43) at 2.2 Angstrom

Hou, J.Chruszcz, M.Shabalin, I.G.Zheng, H.Cooper, D.R.Anderson, W.F.Minor, W.Center for Structural Genomics of Infectious Diseases (CSGID)

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
3-oxoacyl-[acyl-carrier-protein] synthase 2A [auth D],
B [auth A],
C [auth B],
D [auth C]
417Vibrio cholerae O1 biovar El Tor str. N16961Mutation(s): 0 
Gene Names: fabFVC2019VC_2019
EC: 2.3.1.179
UniProt
Find proteins for Q9KQH9 (Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961))
Explore Q9KQH9 
Go to UniProtKB:  Q9KQH9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9KQH9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.543α = 90
b = 136.376β = 90
c = 168.478γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACTdata extraction
HKL-3000data reduction
HKL-3000data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2013-04-03
    Type: Initial release
  • Version 1.1: 2017-11-15
    Changes: Refinement description
  • Version 1.2: 2022-04-13
    Changes: Database references, Derived calculations, Structure summary
  • Version 1.3: 2023-09-20
    Changes: Data collection, Refinement description