3LZB

EGFR kinase domain complexed with an imidazo[2,1-b]thiazole inhibitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.206 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Imidazo[2,1-b]thiazoles: multitargeted inhibitors of both the insulin-like growth factor receptor and members of the epidermal growth factor family of receptor tyrosine kinases.

Fidanze, S.D.Erickson, S.A.Wang, G.T.Mantei, R.Clark, R.F.Sorensen, B.K.Bamaung, N.Y.Kovar, P.Johnson, E.F.Swinger, K.K.Stewart, K.D.Zhang, Q.Tucker, L.A.Pappano, W.N.Wilsbacher, J.L.Wang, J.Sheppard, G.S.Bell, R.L.Davidsen, S.K.Hubbard, R.D.

(2010) Bioorg Med Chem Lett 20: 2452-2455

  • DOI: https://doi.org/10.1016/j.bmcl.2010.03.015
  • Primary Citation of Related Structures:  
    3LZB

  • PubMed Abstract: 

    The design and enzyme activities of a novel class of imidazo[2,1-b]thiazoles is presented.


  • Organizational Affiliation

    Global Pharmaceutical Research and Development, Abbott Laboratories, Abbott Park, IL 60064, USA. steve.fidanze@abbott.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Epidermal growth factor receptor
A, B, C, D, E
A, B, C, D, E, F, G, H
327Homo sapiensMutation(s): 1 
Gene Names: EGFRERBB1
EC: 2.7.10.1
UniProt & NIH Common Fund Data Resources
Find proteins for P00533 (Homo sapiens)
Explore P00533 
Go to UniProtKB:  P00533
PHAROS:  P00533
GTEx:  ENSG00000146648 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00533
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
ITI BindingDB:  3LZB Ki: 32 (nM) from 1 assay(s)
PDBBind:  3LZB IC50: 63 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.206 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 85.586α = 90
b = 70.874β = 109.36
c = 115.182γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
PHASERphasing
BUSTER-TNTrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-03-02
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2021-10-13
    Changes: Database references, Derived calculations
  • Version 1.3: 2023-09-06
    Changes: Data collection, Refinement description