3G11

Structure of E. coli FabF(C163Q) in complex with dihydrophenyl platensimycin

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.168 

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Ligand Structure Quality Assessment 


This is version 2.1 of the entry. See complete history. 


Literature

Synthesis and biological evaluation of platensimycin analogs.

Shen, H.C., Ding, F.X., Singh, S.B., Parthasarathy, G., Soisson, S.M., Ha, S.N., Chen, X., Kodali, S., Wang, J., Dorso, K., Tata, J.R., Hammond, M.L., Maccoss, M., Colletti, S.L.

(2009) Bioorg Med Chem Lett 19: 1623-1627

  • DOI: https://doi.org/10.1016/j.bmcl.2009.02.006
  • Primary Citation of Related Structures:  
    3G0Y, 3G11

  • PubMed Abstract: 

    Platensimycin (1) displays antibacterial activity due to its inhibition of the elongation condensing enzyme (FabF), a novel mode of action that could potentially lead to a breakthrough in developing a new generation of antibiotics. The medicinal chemistry efforts were focused on the modification of the enone moiety of platensimycin and several analogs showed significant activity against FabF and possess antibacterial activity.

    • Organizational Affiliation: 

    Departments of Medicinal Chemistry, Merck Research Laboratories, PO Box 2000, Rahway, NJ 07065-0900, USA.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
3-oxoacyl-[acyl-carrier-protein] synthase 2427Escherichia coli K-12Mutation(s): 1 
Gene Names: b1095, fabF, fabJ, JW1081
EC: 2.3.1.179
UniProt
Find proteins for P0AAI5 (Escherichia coli (strain K12))
Explore P0AAI5 
Go to UniProtKB:  P0AAI5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AAI5
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
P9C
Query on P9C
Download Ideal Coordinates CCD File 
B [auth A]3-({3-[(1S,4S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxo-4-phenyldecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid
C30 H33 N O7
WDRJLSQVOAFEDA-ZORPPZNDSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.168 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.283α = 90
b = 76.283β = 90
c = 146.579γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
TNTrefinement
PDB_EXTRACTdata extraction
ADSCdata collection
BUSTER-TNTrefinement

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-03-17
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-11-01
    Changes: Refinement description
  • Version 2.0: 2021-10-20
    Changes: Atomic model, Database references, Derived calculations
  • Version 2.1: 2023-09-06
    Changes: Data collection, Refinement description