8BO6

COAGULATION FACTOR XI PROTEASE DOMAIN IN COMPLEX WITH ACTIVE SITE INHIBITOR 2


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.25 Å
  • R-Value Free: 0.141 
  • R-Value Work: 0.116 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Design and Preclinical Characterization Program toward Asundexian (BAY 2433334), an Oral Factor XIa Inhibitor for the Prevention and Treatment of Thromboembolic Disorders.

Roehrig, S.Ackerstaff, J.Jimenez Nunez, E.Teller, H.Ellerbrock, P.Meier, K.Heitmeier, S.Tersteegen, A.Stampfuss, J.Lang, D.Schlemmer, K.H.Schaefer, M.Gericke, K.M.Kinzel, T.Meibom, D.Schmidt, M.Gerdes, C.Follmann, M.Hillisch, A.

(2023) J Med Chem 66: 12203-12224

  • DOI: https://doi.org/10.1021/acs.jmedchem.3c00795
  • Primary Citation of Related Structures:  
    8BO3, 8BO4, 8BO5, 8BO6, 8BO7

  • PubMed Abstract: 

    Activated coagulation factor XI (FXIa) is a highly attractive antithrombotic target as it contributes to the development and progression of thrombosis but is thought to play only a minor role in hemostasis so that its inhibition may allow for decoupling of antithrombotic efficacy and bleeding time prolongation. Herein, we report our major efforts to identify an orally bioavailable, reversible FXIa inhibitor. Using a protein structure-based de novo design approach, we identified a novel micromolar hit with attractive physicochemical properties. During lead modification, a critical problem was balancing potency and absorption by focusing on the most important interactions of the lead series with FXIa while simultaneously seeking to improve metabolic stability and the cytochrome P450 interaction profile. In clinical trials, the resulting compound from our extensive research program, asundexian (BAY 2433334), proved to possess the desired DMPK properties for once-daily oral dosing, and even more importantly, the initial pharmacological hypothesis was confirmed.


  • Organizational Affiliation

    Pharmaceuticals, Research and Development, Bayer AG, 42133 Wuppertal, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Coagulation factor XIa light chainA [auth AAA]238Homo sapiensMutation(s): 1 
Gene Names: F11
EC: 3.4.21.27
UniProt & NIH Common Fund Data Resources
Find proteins for P03951 (Homo sapiens)
Explore P03951 
Go to UniProtKB:  P03951
PHAROS:  P03951
GTEx:  ENSG00000088926 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03951
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
QW0 (Subject of Investigation/LOI)
Query on QW0

Download Ideal Coordinates CCD File 
B [auth AAA](~{E})-~{N}-[[5-(3-azanyl-1~{H}-indazol-6-yl)-4-chloranyl-1~{H}-imidazol-2-yl]methyl]-3-[5-chloranyl-2-(1,2,3,4-tetrazol-1-yl)phenyl]prop-2-enamide
C21 H16 Cl2 N10 O
JWIWXNMAPDVMPI-QHHAFSJGSA-N
CIT
Query on CIT

Download Ideal Coordinates CCD File 
C [auth AAA]CITRIC ACID
C6 H8 O7
KRKNYBCHXYNGOX-UHFFFAOYSA-N
GOL
Query on GOL

Download Ideal Coordinates CCD File 
D [auth AAA],
E [auth AAA],
F [auth AAA],
G [auth AAA]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.25 Å
  • R-Value Free: 0.141 
  • R-Value Work: 0.116 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.12α = 90
b = 59.634β = 90
c = 67.053γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Not funded--

Revision History  (Full details and data files)

  • Version 1.0: 2023-09-13
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Database references, Structure summary
  • Version 1.2: 2024-11-20
    Changes: Structure summary