6SEN: TEAD4

Name: PDB 6SEN: TEAD4 bound to a FAM181A peptide
Published: 2019-11-20
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transcription

TEAD4 bound to a FAM181A peptide. Determined by X-ray diffraction at 1.65 Å resolution. Released 20 Nov 2019.

Method: X-ray diffraction
Resolution: 1.65 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,070
Mol. weight: 56.09 kDa
Released: 20 Nov 2019

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

Secondary structure: helices and β-sheets

6SEN 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: 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
α-helix	262-263	2
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 B: 8 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
α-helix	254-255	2
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	368-379	12
α-helix	383-390	8
β-strand	393-401	9	3
β-strand	407-417	11	3
β-strand	425-432	8	3

Chains L and M: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	192-194	3
α-helix	199-202	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcriptional enhancer factor TEF-3	A, B	protein	220	Homo sapiens	Q15561 (AlphaFold model)
Protein FAM181A	L, M	protein	18	Homo sapiens	Q8N9Y4 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6SEN_1 Transcriptional enhancer factor TEF-3 (chains A, B)
GPRSVASSKLWMLEFSAFLEQQQDPDTYNKHLFVHIGQSSPSYSDPYLEAVDIRQIYDKF
PEKKGGLKDLFERGPSNAFFLVKFWADLNTNIEDEGSSFYGVSSQYESPENMIITCSTKV
CSFGKQVVEXVETEYARYENGHYSYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLENFT
ILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE

Sequence of entity 2 (L, M), FASTA

>6SEN_2 Protein FAM181A (chains L, M)
XVPMRKRQLPASFWEEPX

Primary citation

Identification of FAM181A and FAM181B as new interactors with the TEAD transcription factors. Bokhovchuk, F., Mesrouze, Y., Delaunay, C. et al. Protein Sci (2020) 29:509-520. DOI 10.1002/pro.3775 · 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…
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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