7TYU | pdb_00007tyu

TEAD2 bound to Compound 2


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.78 Å
  • R-Value Free: 
    0.230 (Depositor), 0.230 (DCC) 
  • R-Value Work: 
    0.197 (Depositor), 0.200 (DCC) 
  • R-Value Observed: 
    0.199 (Depositor) 

Starting Model: experimental
View more details

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 KTFClick on this verticalbar to view details

This is version 1.1 of the entry. See complete history


Literature

Novel mechanism of YAP-TEAD inhibition results in targeted chromatin remodeling and reveals an expanded Hippo dependent landscape in cancers

Hagenbeek, T.J.Zbieg, J.R.Noland, C.L.Yao, X.Schmidt, S.Clausen, S.Steffek, M.Lee, W.Beroza, P.Martin, S.Lin, E.Fong, R.Di Lello, P.Kubala, M.H.Lacap, J.A.Yang, M.N.Y.Maddalo, D.Lau, J.T.An, L.Levy, E.Lorenzo, M.N.Lee, H.J.Pham, T.H.Modrusan, Z.Zang, R.Chen, Y.C.Li, J.Hafner, M.Chang, M.T.Crawford, J.J.Dey, A.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Transcriptional enhancer factor TEF-4
A, B
231Homo sapiensMutation(s): 0 
Gene Names: TEAD2TEF4
UniProt & NIH Common Fund Data Resources
Find proteins for Q15562 (Homo sapiens)
Explore Q15562 
Go to UniProtKB:  Q15562
PHAROS:  Q15562
GTEx:  ENSG00000074219 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ15562
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.78 Å
  • R-Value Free:  0.230 (Depositor), 0.230 (DCC) 
  • R-Value Work:  0.197 (Depositor), 0.200 (DCC) 
  • R-Value Observed: 0.199 (Depositor) 
Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 115.27α = 90
b = 61.526β = 111.759
c = 79.412γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

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 KTFClick on this verticalbar to view details

Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Other private--

Revision History  (Full details and data files)

  • Version 1.0: 2023-05-03
    Type: Initial release
  • Version 1.1: 2023-10-25
    Changes: Data collection, Refinement description