3NRM

Imidazo[1,2-a]pyrazine-based Aurora Kinase Inhibitors

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.05 Å
  • R-Value Free: 0.258 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.223 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history. 


Literature

Discovery of imidazo[1,2-a]pyrazine-based Aurora kinase inhibitors.

Belanger, D.B., Curran, P.J., Hruza, A., Voigt, J., Meng, Z., Mandal, A.K., Siddiqui, M.A., Basso, A.D., Gray, K.

(2010) Bioorg Med Chem Lett 20: 5170-5174

  • DOI: https://doi.org/10.1016/j.bmcl.2010.07.008
  • Primary Citation of Related Structures:  
    3NRM

  • PubMed Abstract: 

    The synthesis and structure-activity relationships (SAR) of novel, potent imidazo[1,2-a]pyrazine-based Aurora kinase inhibitors are described. The X-ray crystal structure of imidazo[1,2-a]pyrazine Aurora inhibitor 1j is disclosed. Compound 10i was identified as lead compound with a promising overall profile.

    • Organizational Affiliation: 

    Department of Chemistry, Merck Research Laboratories, Cambridge, MA 02141, USA. david.belanger@merck.com


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine/threonine-protein kinase 6283Homo sapiensMutation(s): 2 
Gene Names: AURKA, AIK, ARK1, AURA, BTAK, STK15, STK6
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for O14965 (Homo sapiens)
Explore O14965 
Go to UniProtKB:  O14965
PHAROS:  O14965
GTEx:  ENSG00000087586 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO14965
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NRM
Query on NRM
Download Ideal Coordinates CCD File 
B [auth A]N-(3-methylisothiazol-5-yl)-3-(1H-pyrazol-4-yl)imidazo[1,2-a]pyrazin-8-amine
C13 H11 N7 S
XWFNCZUACYBPGT-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
NRM PDBBind:  3NRM IC50: 4 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.05 Å
  • R-Value Free: 0.258 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.223 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.89α = 90
b = 81.89β = 90
c = 169.271γ = 120
Software Package:
Software NamePurpose
CrystalCleardata collection
BUSTERrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

  • Released Date: 2010-08-18 
    • Deposition Author(s): Hruza, A.

Revision History  (Full details and data files)

  • Version 1.0: 2010-08-18
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description