8YGQ | pdb_00008ygq

Crystal structure of Human TEAD2 in complex with Cobimetinib


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.71 Å
  • R-Value Free: 
    0.257 (Depositor), 0.258 (DCC) 
  • R-Value Work: 
    0.191 (Depositor), 0.193 (DCC) 
  • R-Value Observed: 
    0.198 (Depositor) 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.0 of the entry. See complete history


Literature

Crystal structure of Human TEAD2 in complex with Cobimetinib

He, X.J.Hu, L.Q.Wu, M.Y.

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
226Homo 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
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
EUI (Subject of Investigation/LOI)
Query on EUI

Download Ideal Coordinates CCD File 
D [auth B][3,4-BIS(FLUORANYL)-2-[(2-FLUORANYL-4-IODANYL-PHENYL)AMINO]PHENYL]-[3-OXIDANYL-3-[(2S)-PIPERIDIN-2-YL]AZETIDIN-1-YL]METHANONE
C21 H21 F3 I N3 O2
BSMCAPRUBJMWDF-KRWDZBQOSA-N
PLM
Query on PLM

Download Ideal Coordinates CCD File 
C [auth A]PALMITIC ACID
C16 H32 O2
IPCSVZSSVZVIGE-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.71 Å
  • R-Value Free:  0.257 (Depositor), 0.258 (DCC) 
  • R-Value Work:  0.191 (Depositor), 0.193 (DCC) 
  • R-Value Observed: 0.198 (Depositor) 
Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 122.303α = 90
b = 61.774β = 117.7
c = 80.361γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of China (NSFC)China31970672
National Natural Science Foundation of China (NSFC)China32270877

Revision History  (Full details and data files)

  • Version 1.0: 2025-03-05
    Type: Initial release