1H07 | pdb_00001h07

CDK2 in complex with a disubstituted 4, 6-bis anilino pyrimidine CDK4 inhibitor

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Free: 
    0.235 (Depositor), 0.232 (DCC) 
  • R-Value Work: 
    0.210 (Depositor), 0.210 (DCC) 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 

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

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


Literature

Cyclin-Dependent Kinase 4 Inhibitors as a Treatment for Cancer. Part 1: Identification and Optimisation of Substituted 4,6-Bis Anilino Pyrimidines

Beattie, J.F., Breault, G.A., Ellston, R.P.A., Green, S., Jewsbury, P.J., Midgley, C.J., Naven, R.T., Minshull, C.A., Pauptit, R.A., Tucker, J.A., Pease, J.E.

(2003) Bioorg Med Chem Lett 13: 2955

  • DOI: https://doi.org/10.1016/s0960-894x(03)00202-6
  • Primary Citation of Related Structures:  
    1H00, 1H01, 1H07, 1H08, 1V1K

  • PubMed Abstract: 

    Using a high-throughput screening campaign, we identified the 4,6-bis anilino pyrimidines as inhibitors of the cyclin-dependent kinase, CDK4. Herein we describe the further chemical modification and use of X-ray crystallography to develop potent and selective in vitro inhibitors of CDK4.

    • Organizational Affiliation: 

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


Macromolecules
Find similar proteins by: 
(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
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
MFQ
Query on MFQ
Download Ideal Coordinates CCD File 
C [auth A]((2-BROMO-4-METHYLPHENYL){6-[(4-{[(2S)-3-(DIMETHYLAMINO)-2-HYDROXYPROPYL]OXY}PHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)ACETONITRILE
C24 H27 Br N6 O2
UUISESFNPSRBFN-IBGZPJMESA-N
MFP
Query on MFP
Download Ideal Coordinates CCD File 
B [auth A]((2-BROMO-4-METHYLPHENYL){6-[(4-{[(2R)-3-(DIMETHYLAMINO)-2-HYDROXYPROPYL]OXY}PHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)ACETONITRILE
C24 H27 Br N6 O2
UUISESFNPSRBFN-LJQANCHMSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
MFP BindingDB:  1H07 IC50: 3000 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Free:  0.235 (Depositor), 0.232 (DCC) 
  • R-Value Work:  0.210 (Depositor), 0.210 (DCC) 
Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.323α = 90
b = 71.543β = 90
c = 72.55γ = 90
Software Package:
Software NamePurpose
CNXrefinement
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 MFQClick on this verticalbar to view detailsBest fitted MFPClick 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: 2003-07-11
    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: 2024-10-16
    Changes: Data collection, Database references, Derived calculations, Other, Structure summary