6GEK: TEAD4 (216-434);Y429F

TEAD4 (216-434);Y429F complexed with yap peptide (60-100) and myristoate (covalently bound) at 2.28A (P212121 crystal form); myristoylation was done by adding myr-CoA. Determined by X-ray diffraction at 2.28 Å resolution. Released 19 Sept 2018.

Method: X-ray diffraction
Resolution: 2.28 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,153
Mol. weight: 60.73 kDa
Ligands: MYR
Released: 19 Sept 2018

Explore 6GEK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6GEK contains 21 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: 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	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: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	220	1	1
β-strand	225-236	12	1
β-strand	241-250	10	1
α-helix	259-261	3
β-strand	263-266	4	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	311-322	12	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	368-379	12
α-helix	383-390	8
β-strand	393-401	9	3
β-strand	407-417	11	3
β-strand	425-432	8	3

Chain L: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	61-73	13
α-helix	86-88	3
α-helix	93-95	3

Chain M: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	63-67	5
α-helix	86-88	3
α-helix	93-95	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional enhancer factor TEF-3	A, B	protein	219	Homo sapiens	Q15561 (AlphaFold model)
Transcriptional coactivator YAP1	L, M	protein	41	Homo sapiens	P46937 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6GEK_1 Transcriptional enhancer factor TEF-3 (chains A, B)
GRSVASSKLWMLEFSAFLEQQQDPDTYNKHLFVHIGQSSPSYSDPYLEAVDIRQIYDKFP
EKKGGLKDLFERGPSNAFFLVKFWADLNTNIEDEGSSFYGVSSQYESPENMIITCSTKVC
SFGKQVVEKVETEYARYENGHYSYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLENFTI
LQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIFRLVKE

Sequence of entity 2 (L, M), FASTA

>6GEK_2 Transcriptional coactivator YAP1 (chains L, M)
DSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPE

Ligands and cofactors

ID	Name	Formula	Copies
MYR	Myristic acid	C14 H28 O2	2

Primary citation

Adaptation of the bound intrinsically disordered protein YAP to mutations at the YAP:TEAD interface. Mesrouze, Y., Bokhovchuk, F., Izaac, A. et al. Protein Sci (2018) 27:1810-1820. DOI 10.1002/pro.3493 · 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…
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…

Browse structure collections

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