1TOU

Crystal structure of human adipocyte fatty acid binding protein in complex with a non-covalent ligand

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.204 

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Ligand Structure Quality Assessment 


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


Literature

Substituted benzylamino-6-(trifluoromethyl)pyrimidin-4(1H)-ones: a novel class of selective human A-FABP inhibitors.

Ringom, R., Axen, E., Uppenberg, J., Lundback, T., Rondahl, L., Barf, T.

(2004) Bioorg Med Chem Lett 14: 4449-4452

  • DOI: https://doi.org/10.1016/j.bmcl.2004.06.058
  • Primary Citation of Related Structures:  
    1TOU

  • PubMed Abstract: 

    The synthesis and biological evaluation of novel human A-FABP inhibitors based on the 6-(trifluoromethyl)pyrimidine-4(1H)-one scaffold is described. Two series of compounds, bearing either an amino or carbon substituent in the 2-position of the pyrimidine ring were investigated. Modification of substituents and chain length optimization led to novel compounds with low micromolar activity and good selectivity for human A-FABP.

    • Organizational Affiliation: 

    Department of Medicinal Chemistry, Biovitrum AB, SE-751 37 Uppsala, Sweden.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Fatty acid-binding protein, adipocyte131Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P15090 (Homo sapiens)
Explore P15090 
Go to UniProtKB:  P15090
PHAROS:  P15090
GTEx:  ENSG00000170323 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15090
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
B1V
Query on B1V
Download Ideal Coordinates CCD File 
B [auth A]2-[(2-OXO-2-PIPERIDIN-1-YLETHYL)SULFANYL]-6-(TRIFLUOROMETHYL)PYRIMIDIN-4-OL
C12 H14 F3 N3 O2 S
UDBHGUOSOKOIAX-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
B1V Binding MOAD:  1TOU IC50: 1000 (nM) from 1 assay(s)
PDBBind:  1TOU IC50: 1000 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.204 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 71.829α = 90
b = 53.106β = 90
c = 31.383γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing

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: 2004-08-24
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-03-13
    Changes: Data collection, Database references, Derived calculations