3JUA: YAP recognition by TEAD4 in the Hippo pathway
Structural basis of YAP recognition by TEAD4 in the Hippo pathway. Determined by X-ray diffraction at 3.0 Å resolution. Released 23 Feb 2010.
- Method
- X-ray diffraction
- Resolution
- 3.0 Å
- Organism
- Mus musculus
- Chains
- 8
- Atoms
- 8,055
- Mol. weight
- 120.89 kDa
- Released
- 23 Feb 2010
Explore 3JUA in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3JUA contains 38 α-helices and 52 β-strands across 8 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 | 213 | 1 | 1 |
| β-strand | 218-228 | 11 | 1 |
| β-strand | 233-242 | 10 | 1 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-259 | 3 | 2 |
| α-helix | 260-262 | 3 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-280 | 7 | |
| β-strand | 286-293 | 8 | 2 |
| β-strand | 305-315 | 11 | 1 |
| β-strand | 320-329 | 10 | 2 |
| β-strand | 332-342 | 11 | 2 |
| β-strand | 344-346 | 3 | 1 |
| β-strand | 349-358 | 10 | 1 |
| α-helix | 359-360 | 2 | |
| α-helix | 361-371 | 11 | |
| α-helix | 376-383 | 8 | |
| β-strand | 386-394 | 9 | 2 |
| β-strand | 400-410 | 11 | 2 |
| β-strand | 418-425 | 8 | 2 |
Chain B: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 51-58 | 8 | |
| α-helix | 71-73 | 3 | |
| α-helix | 79-81 | 3 | |
Chain C: 7 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 213 | 1 | 3 |
| β-strand | 218-229 | 12 | 3 |
| β-strand | 233-242 | 10 | 3 |
| β-strand | 256-259 | 4 | 4 |
| α-helix | 260-262 | 3 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-280 | 7 | |
| α-helix | 283-285 | 3 | |
| β-strand | 286-293 | 8 | 4 |
| α-helix | 299-301 | 3 | |
| β-strand | 306-315 | 10 | 3 |
| β-strand | 320-329 | 10 | 4 |
| β-strand | 332-342 | 11 | 4 |
| β-strand | 344-345 | 2 | 3 |
| β-strand | 350-354 | 5 | 3 |
| α-helix | 361-370 | 10 | |
| α-helix | 376-384 | 9 | |
| β-strand | 386-394 | 9 | 4 |
| β-strand | 400-410 | 11 | 4 |
| β-strand | 418-425 | 8 | 4 |
Chain D: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 51-54 | 4 | |
| α-helix | 78-81 | 4 | |
Chain E: 8 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 213 | 1 | 5 |
| β-strand | 218-228 | 11 | 5 |
| β-strand | 234-240 | 7 | 5 |
| α-helix | 253-255 | 3 | |
| β-strand | 256-259 | 4 | 6 |
| α-helix | 260-262 | 3 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-280 | 7 | |
| α-helix | 283-285 | 3 | |
| β-strand | 286-293 | 8 | 6 |
| β-strand | 306-315 | 10 | 5 |
| β-strand | 321-328 | 8 | 6 |
| β-strand | 333-341 | 9 | 6 |
| β-strand | 344-346 | 3 | 5 |
| β-strand | 349-358 | 10 | 5 |
| α-helix | 359-360 | 2 | |
| α-helix | 361-371 | 11 | |
| α-helix | 376-383 | 8 | |
| β-strand | 387-394 | 8 | 6 |
| β-strand | 400-410 | 11 | 6 |
| β-strand | 418-425 | 8 | 6 |
Chain F: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 50-53 | 4 | |
| α-helix | 55-57 | 3 | |
| α-helix | 71-73 | 3 | |
| α-helix | 78-80 | 3 | |
Chain G: 6 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 213 | 1 | 1 |
| β-strand | 218-229 | 12 | 1 |
| β-strand | 233-241 | 9 | 1 |
| β-strand | 257-259 | 3 | 7 |
| α-helix | 260-262 | 3 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-280 | 7 | |
| α-helix | 283-285 | 3 | |
| β-strand | 286-293 | 8 | 7 |
| β-strand | 308-315 | 8 | 1 |
| β-strand | 320-326 | 7 | 7 |
| β-strand | 339-342 | 4 | 7 |
| β-strand | 345 | 1 | 1 |
| β-strand | 350-354 | 5 | 1 |
| α-helix | 361-371 | 11 | |
| α-helix | 376-382 | 7 | |
| β-strand | 387-394 | 8 | 7 |
| β-strand | 400-410 | 11 | 7 |
| β-strand | 418-425 | 8 | 7 |
Chain H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 78-80 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Transcriptional enhancer factor TEF-3 | A, C, E, G | protein | 220 | Mus musculus | Q62296 (AlphaFold model) |
| 65 kDa Yes-associated protein | B, D, F, H | protein | 39 | Mus musculus | P46938 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>3JUA_1 Transcriptional enhancer factor TEF-3 (chains A, C, E, G)
SMRSIASSKLWMLEFSAFLERQQDPDTYNKHLFVHISQSSPSYSDPYLETVDIRQIYDKF
PEKKGGLKELFERGPSNAFFLVKFWADLNTNIDDEGSAFYGVSSQYESPENMIITCSTKV
CSFGKQVVEKVETEYARYENGHYLYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLENFT
ILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE
Sequence of entity 2 (B, D, F, H), FASTA
>3JUA_2 65 kDa Yes-associated protein (chains B, D, F, H)
ETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPE
Primary citation
Structural basis of YAP recognition by TEAD4 in the hippo pathway. Chen, L., Chan, S.W., Zhang, X. et al. Genes Dev (2010) 24:290-300. DOI 10.1101/gad.1865310 · PubMed
Other PDB entries of the same protein (UniProt Q62296 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6SBA 1.3 Å, Crystal Structure of mTEAD with a VGL4 Tertiary Structure Mimetic
- 5XJD 2.22 Å, TEAD in complex with fragment
- 6L9F 2.56 Å, Crystal structure of TEAD4 in complex with a novel FAM181A peptide
- 5Z2Q 2.74 Å, Vgll1-TEAD4 core complex
- 4LN0 2.9 Å, Crystal structure of the VGLL4-TEAD4 complex
- 5GN0 2.9 Å, Structure of TAZ-TEAD complex
Browse structure collections
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