3OT8

X-ray crystal structure of compound 17r bound to human Chk1 kinase domain

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.179 

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Ligand Structure Quality Assessment 


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


Literature

Discovery of pyrazolo[1,5-a]pyrimidine-based CHK1 inhibitors: A template-based approach-Part 1.

Dwyer, M.P., Paruch, K., Labroli, M., Alvarez, C., Keertikar, K.M., Poker, C., Rossman, R., Fischmann, T.O., Duca, J.S., Madison, V., Parry, D., Davis, N., Seghezzi, W., Wiswell, D., Guzi, T.J.

(2011) Bioorg Med Chem Lett 21: 467-470

  • DOI: https://doi.org/10.1016/j.bmcl.2010.10.113
  • Primary Citation of Related Structures:  
    3OT8

  • PubMed Abstract: 

    The synthesis and hit-to-lead SAR development of a pyrazolo[1,5-a]pyrimidine hit 4 is described leading to a series of potent, selective CHK1 inhibitors such as compound 17r. In the Letter, the further utility of the pyrazolo[1,5-a]pyrimidine template for the development of potent, selective kinase inhibitors is detailed.

    • Organizational Affiliation: 

    Merck Research Laboratories, 2015 Galloping Hill Rd, Kenilworth, NJ 07033, USA. michael.dwyer@merck.com


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine/threonine-protein kinase Chk1273Homo sapiensMutation(s): 0 
Gene Names: CHEK1, CHK1
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for O14757 (Homo sapiens)
Explore O14757 
Go to UniProtKB:  O14757
PHAROS:  O14757
GTEx:  ENSG00000149554 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO14757
Sequence Annotations
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  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
MI5 Binding MOAD:  3OT8 IC50: 9 (nM) from 1 assay(s)
BindingDB:  3OT8 IC50: 9 (nM) from 1 assay(s)
PDBBind:  3OT8 IC50: 9 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.179 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 44.78α = 90
b = 65.63β = 94.78
c = 57.64γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
BUSTERrefinement
DENZOdata reduction
SCALEPACKdata scaling
BUSTERphasing

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-11-10
    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