3HMM

Structure of Alk5 + GW855857

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.223 

Starting Model: experimental
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This is version 1.3 of the entry. See complete history. 


Literature

Design of novel quinazoline derivatives and related analogues as potent and selective ALK5 inhibitors

Gellibert, F., Fouchet, M.-H., Nguyen, V.-L., Wang, R., Krysa, G., de Gouville, A.-C., Huet, S., Dodic, N.

(2009) Bioorg Med Chem Lett 19: 2277-2281

  • DOI: https://doi.org/10.1016/j.bmcl.2009.02.087
  • Primary Citation of Related Structures:  
    3GXL, 3HMM

  • PubMed Abstract: 

    Starting from quinazoline 3a, we designed potent and selective ALK5 inhibitors over p38MAP kinase from a rational drug design approach based on co-crystal structures in the human ALK5 kinase domain. The quinazoline 3d exhibited also in vivo activity in an acute rat model of DMN-induced liver fibrosis when administered orally at 5mg/kg (bid).

    • Organizational Affiliation: 

    GlaxoSmithKline, Les Ulis, France. [email protected]


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TGF-beta receptor type-1303Homo sapiensMutation(s): 0 
EC: 2.7.11.30
UniProt & NIH Common Fund Data Resources
Find proteins for P36897 (Homo sapiens)
Explore P36897 
Go to UniProtKB:  P36897
PHAROS:  P36897
GTEx:  ENSG00000106799 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP36897
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
855
Query on 855
Download Ideal Coordinates CCD File 
B [auth A]2-(6-methylpyridin-2-yl)-N-pyridin-4-ylquinazolin-4-amine
C19 H15 N5
JONFDFIXMPXTRH-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
855 BindingDB:  3HMM IC50: min: 25, max: 6720 (nM) from 3 assay(s)
PDBBind:  3HMM IC50: 25 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.223 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42.009α = 90
b = 75.343β = 90
c = 89.678γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNXrefinement
DENZOdata reduction
SCALEPACKdata scaling

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: 2009-06-23
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-11-01
    Changes: Refinement description
  • Version 1.3: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description