9QKQ: HTEAD4 YAP binding domain

Crystal structure of hTEAD4 YAP binding domain (hTEAD4-YBD) in complex with peptide 6. Determined by X-ray diffraction at 1.74 Å resolution. Released 8 Apr 2026.

Method: X-ray diffraction
Resolution: 1.74 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,388
Mol. weight: 56.88 kDa
Ligands: PO4, MYR
Released: 8 Apr 2026

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

Secondary structure: helices and β-sheets

9QKQ contains 20 α-helices and 26 β-strands across 4 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: 9 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	219-220	2	1
β-strand	225-238	14	1
β-strand	241-250	10	1
α-helix	260-263	4
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
α-helix	418-419	2
β-strand	425-432	8	2

Chain B: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	219-220	2	1
β-strand	225-238	14	1
β-strand	241-250	10	1
β-strand	264-266	3	3
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	3
β-strand	312-322	11	1
β-strand	328-336	9	3
β-strand	339-348	10	3
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	3
β-strand	407-417	11	3
α-helix	418-419	2
β-strand	425-432	8	3

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4

Chain D: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
α-helix	10-13	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional enhancer factor TEF-3	A, B	protein	222	Homo sapiens	Q15561 (AlphaFold model)
peptide 6	C, D	protein	17	Homo sapiens

Sequence of entity 1 (A, B), FASTA

>9QKQ_1 Transcriptional enhancer factor TEF-3 (chains A, B)
GSHMRSVASSKLWMLEFSAFLEQQQDPDTYNKHLFVHIGQSSPSYSDPYLEAVDIRQIYD
KFPEKKGGLKDLFERGPSNAFFLVKFWADLNTNIEDEGSSFYGVSSQYESPENMIITCST
KVCSFGKQVVEKVETEYARYENGHYSYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLEN
FTILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE

Sequence of entity 2 (C, D), FASTA

>9QKQ_2 peptide 6 (chains C, D)
XPWRLRKLPDSFAKPPX

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	1
MYR	Myristic acid	C14 H28 O2	2

Water and common crystallization additives (EDO) are not listed.

Primary citation

Deciphering the structural and functional properties of interface 3 and lipidation pocket of hTEAD4 to develop new Hippo Pathway inhibitors through fluorescence anisotropy. Malpezzi, G., Scalvini, L., Tagliazucchi, L. et al. To be published.

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

9SYN 1.3 Å, Crystal structure of TEAD4 in complex with Vgll1-peptide and IAG933
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…
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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