2BZ6

Orally available Factor7a inhibitor

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.193 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.168 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history. 


Literature

Dose-Dependant Antithrombotic Activity of an Orally Active Tissue Factor/Factor Viia Inhibitor without Concomitant Enhancement of Bleeding Propensity.

Groebke-Zbinden, K., Banner, D.W., Hilpert, K., Himber, J., Lave, T., Riederer, M.A., Stahl, M., Tschopp, T.B., Obst-Sander, U.

(2006) Bioorg Med Chem 14: 5357

  • DOI: https://doi.org/10.1016/j.bmc.2006.03.042
  • Primary Citation of Related Structures:  
    2BZ6

  • PubMed Abstract: 

    The discovery of a highly potent and selective tissue factor/factor VIIa inhibitor is described. Upon oral administration of its double prodrug in the guinea pig, a dose-dependent antithrombotic effect is observed in an established model of arterial thrombosis without prolonging bleeding time. The pharmacodynamic properties of this selective inhibitor are compared to the behaviour of a mixed factor VIIa/factor Xa inhibitor.

    • Organizational Affiliation: 

    F. Hoffmann-La Roche Ltd, CH-4070 Basel, Switzerland. katrin.groebke_zbinden@roche.com


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BLOOD COAGULATION FACTOR VIIAA [auth H]254Homo sapiensMutation(s): 0 
EC: 3.4.21.21
UniProt & NIH Common Fund Data Resources
Find proteins for P08709 (Homo sapiens)
Explore P08709 
Go to UniProtKB:  P08709
PHAROS:  P08709
GTEx:  ENSG00000057593 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08709
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
BLOOD COAGULATION FACTOR VIIAB [auth L]53Homo sapiensMutation(s): 0 
EC: 3.4.21.21
UniProt & NIH Common Fund Data Resources
Find proteins for P08709 (Homo sapiens)
Explore P08709 
Go to UniProtKB:  P08709
PHAROS:  P08709
GTEx:  ENSG00000057593 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08709
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
346
Query on 346
Download Ideal Coordinates CCD File 
C [auth H](R)-(4-CARBAMIMIDOYL-PHENYLAMINO)-[5-ETHOXY-2-FLUORO-3-[(R)-TETRAHYDRO-FURAN-3-YLOXY]-PHENYL]-ACETIC ACID
C21 H24 F N3 O5
PGYOHIAQCFZQDK-AUUYWEPGSA-N
SO4
Query on SO4
Download Ideal Coordinates CCD File 
D [auth H]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
CA
Query on CA
Download Ideal Coordinates CCD File 
E [auth H]CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
346 PDBBind:  2BZ6 Ki: 81 (nM) from 1 assay(s)
Binding MOAD:  2BZ6 Ki: 81 (nM) from 1 assay(s)
BindingDB:  2BZ6 Ki: min: 81, max: 88 (nM) from 2 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.193 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.168 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 94.93α = 90
b = 94.93β = 90
c = 115.64γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-02-22
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance