4AQ3

HUMAN BCL-2 WITH PHENYLACYLSULFONAMIDE INHIBITOR


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.245 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.203 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Identification of a Phenylacylsulfonamide Series of Dual Bcl-2/Bcl-Xl Antagonists.

Perez, H.L.Banfi, P.Bertrand, J.A.Cai, Z.W.Grebinski, J.W.Kim, K.Lippy, J.Modugno, M.Naglich, J.Schmidt, R.J.Tebben, A.Vianello, P.Wei, D.D.Zhang, L.Galvani, A.Lombardo, L.J.Borzilleri, R.M.

(2012) Bioorg Med Chem Lett 22: 3946

  • DOI: https://doi.org/10.1016/j.bmcl.2012.04.103
  • Primary Citation of Related Structures:  
    4AQ3

  • PubMed Abstract: 

    A series of phenylacylsulfonamides has been prepared as antagonists of Bcl-2/Bcl-xL. In addition to potent binding affinities for both Bcl-2 and Bcl-xL, these compounds were shown to induce classical markers of apoptosis in isolated mitochondria. Overall weak cellular potency was improved by the incorporation of polar functionality resulting in compounds with moderate antiproliferative activity.


  • Organizational Affiliation

    Bristol-Myers Squibb Research, PO Box 4000, Princeton, NJ 08543, USA. heidi.perez@bms.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
APOPTOSIS REGULATOR BCL-2, BCL-2-LIKE PROTEIN 1
A, B, C, D, E
A, B, C, D, E, F
169Homo sapiensMutation(s): 2 
UniProt & NIH Common Fund Data Resources
Find proteins for Q07817 (Homo sapiens)
Explore Q07817 
Go to UniProtKB:  Q07817
PHAROS:  Q07817
GTEx:  ENSG00000171552 
Find proteins for P10415 (Homo sapiens)
Explore P10415 
Go to UniProtKB:  P10415
PHAROS:  P10415
GTEx:  ENSG00000171791 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsQ07817P10415
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
398 PDBBind:  4AQ3 IC50: 37 (nM) from 1 assay(s)
Binding MOAD:  4AQ3 IC50: 37 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.245 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.203 
  • Space Group: P 32
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 115.214α = 90
b = 115.214β = 90
c = 102.318γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata 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: 2012-06-06
    Type: Initial release
  • Version 1.1: 2012-11-21
    Changes: Database references