2P83

Potent and selective isophthalamide S2 hydroxyethylamine inhibitor of BACE1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.207 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Potent and selective isophthalamide S(2) hydroxyethylamine inhibitors of BACE1.

Kortum, S.W.Benson, T.E.Bienkowski, M.J.Emmons, T.L.Prince, D.B.Paddock, D.J.Tomasselli, A.G.Moon, J.B.Laborde, A.Tenbrink, R.E.

(2007) Bioorg Med Chem Lett 17: 3378-3383

  • DOI: https://doi.org/10.1016/j.bmcl.2007.03.096
  • Primary Citation of Related Structures:  
    2P83

  • PubMed Abstract: 

    The design and synthesis of a novel series of potent BACE1 hydroxyethylamine inhibitors. These inhibitors feature hydrogen bonding substituents at the C-5 position of the isophthalamide ring with improved selectivity over cathepsin D.


  • Organizational Affiliation

    Pfizer Global Research and Development, Pfizer Inc., St. Louis Laboratories, 700 Chesterfield Parkway West, Chesterfield, MO 63017, USA. steve.kortum@pfizer.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-secretase 1
A, B, C
455Homo sapiensMutation(s): 0 
Gene Names: BACE1BACE
EC: 3.4.23.46
UniProt & NIH Common Fund Data Resources
Find proteins for P56817 (Homo sapiens)
Explore P56817 
Go to UniProtKB:  P56817
PHAROS:  P56817
GTEx:  ENSG00000186318 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP56817
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
MR0 Binding MOAD:  2P83 IC50: 11 (nM) from 1 assay(s)
BindingDB:  2P83 IC50: 11 (nM) from 1 assay(s)
PDBBind:  2P83 IC50: 11 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.207 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.96α = 90
b = 103.35β = 104.12
c = 101.01γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction
X-PLORphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-06-19
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description