8EME | pdb_00008eme

EGFR(T790M/V948R) in complex with ZNL-0056


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.32 Å
  • R-Value Free: 
    0.318 (Depositor), 0.310 (DCC) 
  • R-Value Work: 
    0.283 (Depositor), 0.290 (DCC) 
  • R-Value Observed: 
    0.285 (Depositor) 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted ZNLClick on this verticalbar to view details

This is version 1.3 of the entry. See complete history


Literature

Molecular Bidents with Two Electrophilic Warheads as a New Pharmacological Modality.

Li, Z.Jiang, J.Ficarro, S.B.Beyett, T.S.To, C.Tavares, I.Zhu, Y.Li, J.Eck, M.J.Janne, P.A.Marto, J.A.Zhang, T.Che, J.Gray, N.S.

(2024) ACS Cent Sci 10: 1156-1166

  • DOI: https://doi.org/10.1021/acscentsci.3c01245
  • Primary Citation of Related Structures:  
    8EME

  • PubMed Abstract: 

    A systematic strategy to develop dual-warhead inhibitors is introduced to circumvent the limitations of conventional covalent inhibitors such as vulnerability to mutations of the corresponding nucleophilic residue. Currently, all FDA-approved covalent small molecules feature one electrophile, leaving open a facile route to acquired resistance. We conducted a systematic analysis of human proteins in the protein data bank to reveal ∼400 unique targets amendable to dual covalent inhibitors, which we term "molecular bidents". We demonstrated this strategy by targeting two kinases: MKK7 and EGFR. The designed compounds, ZNL-8162 and ZNL-0056, are ATP-competitive inhibitors that form two covalent bonds with cysteines and retain potency against single cysteine mutants. Therefore, molecular bidents represent a new pharmacological modality with the potential for improved selectivity, potency, and drug resistance profile.


  • Organizational Affiliation

    Department of Chemical and Systems Biology, Stanford Cancer Institute, ChEM-H, Stanford University, Stanford, California 94305, United States.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Epidermal growth factor receptorA [auth B],
B [auth A]
331Homo sapiensMutation(s): 2 
Gene Names: EGFRERBBERBB1HER1
EC: 2.7.10.1
UniProt & NIH Common Fund Data Resources
Find proteins for P00533 (Homo sapiens)
Explore P00533 
Go to UniProtKB:  P00533
PHAROS:  P00533
GTEx:  ENSG00000146648 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00533
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZNL (Subject of Investigation/LOI)
Query on ZNL

Download Ideal Coordinates CCD File 
C [auth B]N-{7-methyl-1-[(3S)-1-(prop-2-enoyl)azepan-3-yl]-1H-benzimidazol-2-yl}-5-(prop-2-enamido)thiophene-3-carboxamide
C25 H27 N5 O3 S
DZTGCJZKRUDIGP-SFHVURJKSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.32 Å
  • R-Value Free:  0.318 (Depositor), 0.310 (DCC) 
  • R-Value Work:  0.283 (Depositor), 0.290 (DCC) 
  • R-Value Observed: 0.285 (Depositor) 
Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 34.874α = 90
b = 99.992β = 100.8
c = 87.023γ = 90
Software Package:
Software NamePurpose
xia2data scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
xia2data reduction
PHASERphasing
Cootmodel building

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted ZNLClick on this verticalbar to view details

Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Cancer Institute (NIH/NCI)United States5R01CA116020-16

Revision History  (Full details and data files)

  • Version 1.0: 2023-10-18
    Type: Initial release
  • Version 1.1: 2024-03-06
    Changes: Database references
  • Version 1.2: 2024-07-10
    Changes: Database references
  • Version 1.3: 2024-11-13
    Changes: Structure summary