9SYN: TEAD4

Crystal structure of TEAD4 in complex with Vgll1-peptide and IAG933. Determined by X-ray diffraction at 1.3 Å resolution. Released 11 Mar 2026.

Method: X-ray diffraction
Resolution: 1.3 Å
Organisms: Homo sapiens, Mus musculus
Chains: 2
Atoms: 2,076
Mol. weight: 28.29 kDa
Ligands: MYR, WCF
Released: 11 Mar 2026

Explore 9SYN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9SYN contains 8 α-helices and 13 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	219-220	2	1
β-strand	225-235	11	1
β-strand	244-249	6	1
β-strand	264-266	3	2
α-helix	267-269	3
α-helix	271-273	3
α-helix	281-287	7
α-helix	290-292	3
β-strand	293-300	8	2
β-strand	312-322	11	1
β-strand	327-336	10	2
β-strand	339-349	11	2
β-strand	351-353	3	1
β-strand	356-365	10	1
α-helix	366-367	2
α-helix	368-378	11
α-helix	383-390	8
β-strand	393-401	9	2
β-strand	407-417	11	2
β-strand	425-432	8	2

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	37-50	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional enhancer factor TEF-3	A	protein	220	Homo sapiens	Q15561 (AlphaFold model)
Transcription cofactor vestigial-like protein 1	B	protein	18	Mus musculus	Q99NC0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9SYN_1 Transcriptional enhancer factor TEF-3 (chains A)
GPRSVASSKLWMLEFSAFLEQQQDPDTYNKHLFVHIGQSSPSYSDPYLEAVDIRQIYDKF
PEKKGGLKDLFERGPSNAFFLVKFWADLNTNIEDEGSSFYGVSSQYESPENMIITCSTKV
CSFGKQVVEKVETEYARYENGHYSYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLENFT
ILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE

Sequence of entity 2 (B), FASTA

>9SYN_2 Transcription cofactor vestigial-like protein 1 (chains B)
XDINSMVDEHFSRALRNX

Ligands and cofactors

ID	Name	Formula	Copies
MYR	Myristic acid	C14 H28 O2	1
WCF	4-[(2~{S})-5-chloranyl-6-fluoranyl-2-phenyl-2-[(2~{S})-pyrrolidin-2-yl]-3~{H}-1…	C27 H26 Cl F2 N3 O4	1

Primary citation

Discovery of Clinical Candidate IAG933, a Potent YAP-TEAD PPI Disrupter. Vogtle, M., Sellner, H., Chapeau, E. et al. J Med Chem (2026) 69:7782-7816. DOI 10.1021/acs.jmedchem.5c03009 · PubMed

Other PDB entries of the same protein (UniProt Q15561 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6GEI 1.65 Å, TEAD4 (216-434);E263A+Y429F complexed with yap peptide (60- 100);S94A and myristoate…
6HIK 1.65 Å, X-ray structure of TEAD4(Y429H) mutant) complexed with YAP (wildtype): Molecular and…
6SEN 1.65 Å, TEAD4 bound to a FAM181A peptide
8A8R 1.7 Å, Crystal structure of TEAD4 in complex with YAP peptide
6GEC 1.7 Å, TEAD4 (216-434) complexed with yap peptide (60-100);S94A and myristoate (covalently…
9QKQ 1.74 Å, Crystal structure of hTEAD4 YAP binding domain (hTEAD4-YBD) in complex with peptide 6
6GE6 1.8 Å, X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(wildtype): The role of…
6GE3 1.85 Å, X-ray structure of TEAD4 (wildtype) complexed with YAP (wildtype): The role of residual…
5OAQ 1.95 Å, TEAD4 complexed with yap peptide and myristate (covalently bound)
6GEE 1.96 Å, TEAD4 (216-434);E263A complexed with yap peptide (60-100); S94A and myristoate…
6GE4 1.97 Å, TEAD4 (216-434);E263A complexed with yap peptide (60-100) and myristoate (covalently…
8CAA 2.0 Å, Crystal structure of TEAD4 in complex with YTP-13

Browse structure collections

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