1OIT | pdb_00001oit

Imidazopyridines: a potent and selective class of Cyclin-dependent Kinase inhibitors identified through Structure-based hybridisation

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 
    0.240 (Depositor), 0.250 (DCC) 
  • R-Value Work: 
    0.226 (Depositor), 0.240 (DCC) 
  • R-Value Observed: 
    0.227 (Depositor) 

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Ligand Structure Quality Assessment 

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This is version 1.4 of the entry. See complete history. 


Literature

Imidazo[1,2-A]Pyridines: A Potent and Selective Class of Cyclin-Dependent Kinase Inhibitors Identified Through Structure-Based Hybridisation

Anderson, M., Beattie, J.F., Breault, G.A., Breed, J., Byth, K.F., Culshaw, J.D., Ellston, R.P.A., Green, S., Minshull, C.A., Norman, R.A., Pauptit, R.A., Stanway, J., Thomas, A.P., Jewsbury, P.J.

(2003) Bioorg Med Chem Lett 13: 3021

  • DOI: https://doi.org/10.1016/s0960-894x(03)00638-3
  • Primary Citation of Related Structures:  
    1OIQ, 1OIR, 1OIT

  • PubMed Abstract: 

    High-throughput screening identified the imidazo[1,2-a]pyridine and bisanilinopyrimidine series as inhibitors of the cyclin-dependent kinase CDK4. Comparison of their experimentally-determined binding modes and emerging structure-activity trends led to the development of potent and selective imidazo[1,2-a]pyridine inhibitors for CDK4 and in particular CDK2.

    • Organizational Affiliation: 

    AstraZeneca, Alderley Park, Macclesfield, Cheshire SK10 4TG, UK.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CELL DIVISION PROTEIN KINASE 2299Homo sapiensMutation(s): 0 
EC: 2.7.1.37 (PDB Primary Data), 2.7.11.22 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for P24941 (Homo sapiens)
Explore P24941 
Go to UniProtKB:  P24941
PHAROS:  P24941
GTEx:  ENSG00000123374 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP24941
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
HDT
Query on HDT
Download Ideal Coordinates CCD File 
B [auth A]4-[(4-IMIDAZO[1,2-A]PYRIDIN-3-YLPYRIMIDIN-2-YL)AMINO]BENZENESULFONAMIDE
C17 H14 N6 O2 S
NKORVPQBJCGYEC-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
HDT BindingDB:  1OIT IC50: min: 1, max: 3 (nM) from 3 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free:  0.240 (Depositor), 0.250 (DCC) 
  • R-Value Work:  0.226 (Depositor), 0.240 (DCC) 
  • R-Value Observed: 0.227 (Depositor) 
Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.466α = 90
b = 72.239β = 90
c = 72.227γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted HDTClick on this verticalbar to view details

View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-09-04
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-05-08
    Changes: Data collection, Database references, Other
  • Version 1.4: 2024-11-13
    Changes: Structure summary