Research workbench
TEAD4-HOXB13 complex bound to DNA
Analyse TEAD4-HOXB13 complex bound to DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NO6
- Type
- protein + DNA
- Length
- 339 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q92826, Q15561
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 62 | — | Q92826 |
| C, D | — | dna | 18 | — | — |
| F, E | — | dna | 18 | — | — |
| I | — | protein | 70 | — | Q15561 |
| N | — | protein | 73 | — | Q15561 |
Compared structures
- 5NO6 · TEAD4-HOXB13 complex bound to DNA · the same entry in another collection · chain N against N, TM-score 1.00
- Q92826 · AlphaFold monomer V2.0 prediction for homeobox protein hox-B13 (Q92826) · a predicted model of the same protein · chain A against A, TM-score 0.92
- Q15561 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-3 (Q15561) · a predicted model of the same protein · chain N against A, TM-score 0.84
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 Q92826
- Every structure of UniProt Q15561
- Elsewhere: RCSB PDB 5NO6 · PDBe 5NO6 · UniProt Q92826 · UniProt Q15561
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