5OAQ: TEAD4

TEAD4 complexed with yap peptide and myristate (covalently bound). Determined by X-ray diffraction at 1.95 Å resolution. Released 11 Oct 2017.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,172
Mol. weight: 30.57 kDa
Ligands: MYR
Released: 11 Oct 2017

Explore 5OAQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5OAQ contains 11 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	220	1	1
β-strand	225-238	14	1
β-strand	241-250	10	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	328-336	9	2
β-strand	339-348	10	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 L: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	65-73	9
α-helix	75-77	3
α-helix	86-88	3
α-helix	93-96	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional enhancer factor TEF-3	A	protein	220	Homo sapiens	Q15561 (AlphaFold model)
Transcriptional coactivator YAP1	L	protein	41	Homo sapiens	P46937 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5OAQ_1 Transcriptional enhancer factor TEF-3 (chains A)
GPRSVASSKLWMLEFSAFLEQQQDPDTYNKHLFVHIGQSSPSYSDPYLEAVDIRQIYDKF
PEKKGGLKDLFERGPSNAFFLVKFWADLNTNIEDEGSSFYGVSSQYESPENMIITCSTKV
CSFGKQVVEKVETEYARYENGHYSYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLENFT
ILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE

Sequence of entity 2 (L), FASTA

>5OAQ_2 Transcriptional coactivator YAP1 (chains L)
DSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPE

Ligands and cofactors

ID	Name	Formula	Copies
MYR	Myristic acid	C14 H28 O2	1

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

Primary citation

Effect of the acylation of TEAD4 on its interaction with co-activators YAP and TAZ. Mesrouze, Y., Meyerhofer, M., Bokhovchuk, F. et al. Protein Sci (2017) 26:2399-2409. DOI 10.1002/pro.3312 · PubMed

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…
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…
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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