4ANQ

Structure of G1269A Mutant Anaplastic Lymphoma Kinase in Complex with Crizotinib


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.76 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.201 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Design of Potent and Selective Inhibitors to Overcome Clinical Anaplastic Lymphoma Kinase Mutations Resistant to Crizotinib.

Huang, Q.Johnson, T.W.Bailey, S.Brooun, A.Bunker, K.D.Burke, B.J.Collins, M.R.Cook, A.S.Cui, J.J.Dack, K.N.Deal, J.G.Deng, Y.Dinh, D.Engstrom, L.D.He, M.Hoffman, J.Hoffman, R.L.Johnson, P.S.Kania, R.S.Lam, H.Lam, J.L.Le, P.T.Li, Q.Lingardo, L.Liu, W.Lu, M.W.Mctigue, M.Palmer, C.L.Richardson, P.F.Sach, N.W.Shen, H.Smeal, T.Smith, G.L.Stewart, A.E.Timofeevski, S.Tsaparikos, K.Wang, H.Zhu, H.Zhu, J.Zou, H.Y.Edwards, M.P.

(2014) J Med Chem 57: 1170

  • DOI: https://doi.org/10.1021/jm401805h
  • Primary Citation of Related Structures:  
    2YFX, 2YHV, 4ANL, 4ANQ, 4CCB, 4CCU, 4CD0

  • PubMed Abstract: 

    Crizotinib (1), an anaplastic lymphoma kinase (ALK) receptor tyrosine kinase inhibitor approved by the U.S. Food and Drug Administration in 2011, is efficacious in ALK and ROS positive patients. Under pressure of crizotinib treatment, point mutations arise in the kinase domain of ALK, resulting in resistance and progressive disease. The successful application of both structure-based and lipophilic-efficiency-focused drug design resulted in aminopyridine 8e, which was potent across a broad panel of engineered ALK mutant cell lines and showed suitable preclinical pharmacokinetics and robust tumor growth inhibition in a crizotinib-resistant cell line (H3122-L1196M).


  • Organizational Affiliation

    La Jolla Laboratories, Pfizer Worldwide Research and Development , 10770 Science Center Drive, San Diego, California 92121, United States.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ALK TYROSINE KINASE RECEPTOR342Homo sapiensMutation(s): 1 
EC: 2.7.10.1
UniProt & NIH Common Fund Data Resources
Find proteins for Q9UM73 (Homo sapiens)
Explore Q9UM73 
Go to UniProtKB:  Q9UM73
PHAROS:  Q9UM73
GTEx:  ENSG00000171094 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9UM73
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
VGH
Query on VGH

Download Ideal Coordinates CCD File 
B [auth A]3-[(1R)-1-(2,6-dichloro-3-fluorophenyl)ethoxy]-5-(1-piperidin-4-yl-1H-pyrazol-4-yl)pyridin-2-amine
C21 H22 Cl2 F N5 O
KTEIFNKAUNYNJU-GFCCVEGCSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
VGH BindingDB:  4ANQ Ki: min: 0.74, max: 8.2 (nM) from 2 assay(s)
Kd: min: 3.3, max: 4.4 (nM) from 3 assay(s)
IC50: min: 0.64, max: 3039 (nM) from 66 assay(s)
EC50: min: 575, max: 2.28e+4 (nM) from 3 assay(s)
Binding MOAD:  4ANQ IC50: 605 (nM) from 1 assay(s)
PDBBind:  4ANQ IC50: 605 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.76 Å
  • R-Value Free: 0.217 
  • R-Value Work: 0.201 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 51.626α = 90
b = 57.473β = 90
c = 104.617γ = 90
Software Package:
Software NamePurpose
CNXrefinement
autoPROCdata reduction
SCALAdata scaling
CNXphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-03-27
    Type: Initial release
  • Version 1.1: 2014-03-19
    Changes: Atomic model, Database references
  • Version 1.2: 2019-05-08
    Changes: Data collection, Experimental preparation, Other
  • Version 1.3: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description