5A5O

Crystal structure of human ATAD2 bromodomain in complex with 3-methyl- 1,2-dihydroquinolin-2-one


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.04 Å
  • R-Value Free: 0.199 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.178 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Fragment-Based Discovery of Low-Micromolar Atad2 Bromodomain Inhibitors.

Demont, E.H.Chung, C.Furze, R.C.Grandi, P.Michon, A.Wellaway, C.Barrett, N.Bridges, A.M.Craggs, P.D.Diallo, H.Dixon, D.P.Douault, C.Emmons, A.J.Jones, E.J.Karamshi, B.V.Locke, K.Mitchell, D.J.Mouzon, B.H.Prinjha, R.K.Roberts, A.D.Sheppard, R.J.Watson, R.J.Bamborough, P.

(2015) J Med Chem 58: 5649

  • DOI: https://doi.org/10.1021/acs.jmedchem.5b00772
  • Primary Citation of Related Structures:  
    5A5N, 5A5O, 5A5P, 5A5Q, 5A5R, 5A5S

  • PubMed Abstract: 

    Overexpression of ATAD2 (ATPase family, AAA domain containing 2) has been linked to disease severity and progression in a wide range of cancers, and is implicated in the regulation of several drivers of cancer growth. Little is known of the dependence of these effects upon the ATAD2 bromodomain, which has been categorized as among the least tractable of its class. The absence of any potent, selective inhibitors limits clear understanding of the therapeutic potential of the bromodomain. Here, we describe the discovery of a hit from a fragment-based targeted array. Optimization of this produced the first known micromolar inhibitors of the ATAD2 bromodomain.


  • Organizational Affiliation

    §Molecular Discovery Research, Cellzome GmbH, GlaxoSmithKline, Meyerhofstrasse 1, 69117 Heidelberg, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATPASE FAMILY AAA DOMAIN-CONTAINING PROTEIN 2130Homo sapiensMutation(s): 0 
EC: 3.6.1.3 (PDB Primary Data), 3.6.1 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for Q6PL18 (Homo sapiens)
Explore Q6PL18 
Go to UniProtKB:  Q6PL18
PHAROS:  Q6PL18
GTEx:  ENSG00000156802 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6PL18
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.04 Å
  • R-Value Free: 0.199 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.178 
  • Space Group: P 65 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.423α = 90
b = 79.423β = 90
c = 137.198γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
SCALAdata scaling

Structure Validation

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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: 2015-08-05
    Changes: Database references
  • Version 1.2: 2024-05-08
    Changes: Data collection, Database references, Derived calculations, Other