5HZ5

FABP5 in complex with 6-Chloro-4-phenyl-2-piperidin-1-yl-3-(1H-tetrazol-5-yl)-quinoline


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.208 
  • R-Value Observed: 0.209 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Design and synthesis of selective, dual fatty acid binding protein 4 and 5 inhibitors.

Kuhne, H.Obst-Sander, U.Kuhn, B.Conte, A.Ceccarelli, S.M.Neidhart, W.Rudolph, M.G.Ottaviani, G.Gasser, R.So, S.S.Li, S.Zhang, X.Gao, L.Myers, M.

(2016) Bioorg Med Chem Lett 26: 5092-5097

  • DOI: https://doi.org/10.1016/j.bmcl.2016.08.071
  • Primary Citation of Related Structures:  
    5HZ5, 5HZ6, 5HZ8, 5HZ9

  • PubMed Abstract: 

    Dual inhibition of fatty acid binding proteins 4 and 5 (FABP4 and FABP5) is expected to provide beneficial effects on a number of metabolic parameters such as insulin sensitivity and blood glucose levels and should protect against atherosclerosis. Starting from a FABP4 selective focused screening hit, biostructure information was used to modulate the selectivity profile in the desired way and to design potent dual FABP4/5 inhibitors with good selectivity against FABP3. With very good pharmacokinetic properties and no major safety alerts, compound 12 was identified as a suitable tool compound for further in vivo investigations.


  • Organizational Affiliation

    Roche Pharmaceutical Research and Early Development, Roche Innovation Center Basel, F. Hoffmann-La Roche Ltd, 4070 Basel, Switzerland. Electronic address: [email protected].


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Fatty acid-binding protein, epidermal134Homo sapiensMutation(s): 0 
Gene Names: FABP5
UniProt & NIH Common Fund Data Resources
Find proteins for Q01469 (Homo sapiens)
Explore Q01469 
Go to UniProtKB:  Q01469
PHAROS:  Q01469
GTEx:  ENSG00000164687 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ01469
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
65X BindingDB:  5HZ5 Ki: 86 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.208 
  • R-Value Observed: 0.209 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 62.79α = 90
b = 62.79β = 90
c = 75.35γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PDB_EXTRACTdata extraction
PHENIXrefinement
XDSdata reduction
REFMACphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-01-25
    Type: Initial release
  • Version 1.1: 2017-10-11
    Changes: Data collection
  • Version 1.2: 2024-11-13
    Changes: Data collection, Database references, Structure summary