Research workbench
Structural basis of yap recognition by TEAD4 in the hippo pathway
Analyse Structural basis of yap recognition by TEAD4 in the hippo pathway in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JUA
- Type
- protein
- Length
- 952 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q62296, P46938
Structure
x-ray diffraction · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 204 | — | Q62296 |
| B | — | protein | 39 | — | P46938 |
| C | — | protein | 213 | — | Q62296 |
| D | — | protein | 35 | — | P46938 |
| E | — | protein | 216 | — | Q62296 |
| F | — | protein | 36 | — | P46938 |
| G | — | protein | 190 | — | Q62296 |
| H | — | protein | 19 | — | P46938 |
Compared structures
- 3JUA · Structural basis of YAP recognition by TEAD4 in the Hippo pathway · the same entry in another collection · chain H against H, TM-score 1.00
- Q62296 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-3 (Q62296) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q62296
- Every structure of UniProt P46938
- Elsewhere: RCSB PDB 3JUA · PDBe 3JUA · UniProt Q62296 · UniProt P46938
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