4USF

Human SLK with SB-440719


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.198 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Comprehensive Characterization of the Published Kinase Inhibitor Set.

Elkins, J.M.Fedele, V.Szklarz, M.Abdul Azeez, K.R.Salah, E.Mikolajczyk, J.Romanov, S.Sepetov, N.Huang, X.P.Roth, B.L.Al Haj Zen, A.Fourches, D.Muratov, E.Tropsha, A.Morris, J.Teicher, B.A.Kunkel, M.Polley, E.Lackey, K.E.Atkinson, F.L.Overington, J.P.Bamborough, P.Moller, S.Price, D.J.Willson, T.M.Drewry, D.H.Knapp, S.Zuercher, W.J.

(2016) Nat Biotechnol 34: 95

  • DOI: https://doi.org/10.1038/nbt.3374
  • Primary Citation of Related Structures:  
    4USD, 4USE, 4USF

  • PubMed Abstract: 

    Despite the success of protein kinase inhibitors as approved therapeutics, drug discovery has focused on a small subset of kinase targets. Here we provide a thorough characterization of the Published Kinase Inhibitor Set (PKIS), a set of 367 small-molecule ATP-competitive kinase inhibitors that was recently made freely available with the aim of expanding research in this field and as an experiment in open-source target validation. We screen the set in activity assays with 224 recombinant kinases and 24 G protein-coupled receptors and in cellular assays of cancer cell proliferation and angiogenesis. We identify chemical starting points for designing new chemical probes of orphan kinases and illustrate the utility of these leads by developing a selective inhibitor for the previously untargeted kinases LOK and SLK. Our cellular screens reveal compounds that modulate cancer cell growth and angiogenesis in vitro. These reagents and associated data illustrate an efficient way forward to increasing understanding of the historically untargeted kinome.


  • Organizational Affiliation

    Structural Genomics Consortium and Target Discovery Institute, Nuffield Department of Clinical Medicine, Old Road Campus, University of Oxford, Oxford, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
STE20-LIKE SERINE/THREONINE-PROTEIN KINASE
A, B
304Homo sapiensMutation(s): 0 
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for Q9H2G2 (Homo sapiens)
Explore Q9H2G2 
Go to UniProtKB:  Q9H2G2
PHAROS:  Q9H2G2
GTEx:  ENSG00000065613 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9H2G2
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
6UI
Query on 6UI

Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]
4-[4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
C19 H15 N3 O
DXOWEAIMGARAMG-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.198 
  • Space Group: P 2 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.94α = 90
b = 75.3β = 90
c = 189.57γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-07-22
    Type: Initial release
  • Version 1.1: 2015-11-04
    Changes: Database references
  • Version 1.2: 2016-01-20
    Changes: Database references
  • Version 1.3: 2018-01-24
    Changes: Structure summary