3O23

Human unphosphorylated IGF1-R Kinase domain in complex with an hydantoin inhibitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.278 
  • R-Value Work: 0.238 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Discovery of the first non-ATP competitive IGF-1R kinase inhibitors: Advantages in comparison with competitive inhibitors

Lesuisse, D.Mauger, J.Nemecek, C.Maignan, S.Boiziau, J.Harlow, G.Hittinger, A.Ruf, S.Strobel, H.Nair, A.Ritter, K.Malleron, J.L.Dagallier, A.El-Ahmad, Y.Guilloteau, J.P.Guizani, H.Bouchard, H.Venot, C.

(2011) Bioorg Med Chem Lett 21: 2224-2228

  • DOI: https://doi.org/10.1016/j.bmcl.2011.03.003
  • Primary Citation of Related Structures:  
    3O23

  • PubMed Abstract: 

    A new series of IGF-1R inhibitors related to hydantoins were identified from a lead originating from HTS. Their noncompetitive property as well as their slow binding characteristics provided a series of compounds with unique selectivity and excellent cellular activities.


  • Organizational Affiliation

    Medicinal Chemistry, Sanofi-aventis, 13 Quai Jules Guesde, 94300 Vitry-sur-Seine, France. dominique.lesuisse@sanofi-aventis.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Insulin-like growth factor 1 receptor305Homo sapiensMutation(s): 1 
Gene Names: IGF1R
EC: 2.7.10.1
UniProt & NIH Common Fund Data Resources
Find proteins for P08069 (Homo sapiens)
Explore P08069 
Go to UniProtKB:  P08069
PHAROS:  P08069
GTEx:  ENSG00000140443 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08069
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
MQY
Query on MQY

Download Ideal Coordinates CCD File 
B [auth A](5S)-5-methyl-1-(quinolin-4-ylmethyl)-3-{4-[(trifluoromethyl)sulfonyl]phenyl}imidazolidine-2,4-dione
C21 H16 F3 N3 O4 S
GKQIKYWYJQQLLD-ZDUSSCGKSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
MQY PDBBind:  3O23 IC50: 500 (nM) from 1 assay(s)
Binding MOAD:  3O23 IC50: 500 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.278 
  • R-Value Work: 0.238 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.768α = 90
b = 48.755β = 98.74
c = 70.73γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNXrefinement

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-05-04
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description