Research workbench
Structure of TAZ-TEAD complex
Analyse Structure of TAZ-TEAD complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GN0
- Type
- protein
- Length
- 1,014 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Mus musculus
- Molecule
- Transcriptional enhancer factor TEF-3; WW domain-containing transcription regulator…
- UniProt
- Q62296, Q9EPK5
- Ligands
- PLM
- Pockets
- 18 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.9 · 5 distinct chains · 18% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Transcriptional enhancer factor TEF-3 | protein | 222 | 16% helix, 47% strand | Q62296 |
| D | Transcriptional enhancer factor TEF-3 | protein | 221 | 18% helix, 47% strand | Q62296 |
| E, H | WW domain-containing transcription regulator protein 1 | protein | 32 | 28% helix, 6% strand | Q9EPK5 |
| F | WW domain-containing transcription regulator protein 1 | protein | 30 | 13% helix, 0% strand | Q9EPK5 |
| G | WW domain-containing transcription regulator protein 1 | protein | 33 | 21% helix, 0% strand | Q9EPK5 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 3 copies · chains B, C, D
- CIT · Citric acid · additive · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 347 | 0.81 | 0.90 | 41 | empty |
| 2 | 292 | 0.81 | 0.91 | 39 | PLM |
| 3 | 316 | 0.80 | 0.90 | 39 | PLM |
| 4 | 365 | 0.79 | 0.88 | 47 | PLM |
| 5 | 490 | 0.59 | 0.74 | 54 | CIT |
Interfaces
9 interfaces between chains.
- B–G · 1372 Ų buried · 7 hydrogen bonds · protein-protein
- D–H · 1276 Ų buried · 12 hydrogen bonds · protein-protein
- C–F · 873 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 804 Ų buried · 16 hydrogen bonds · protein-protein
- A–E · 797 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 lipid (palmitoylation).
Compared structures
- 5GN0 · Structure of taz-tead complex · 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 D against A, TM-score 0.97
- Q9EPK5 · AlphaFold monomer V2.0 prediction for ww domain-containing transcription regulator… · a predicted model of the same protein · chain G against A, TM-score 0.59
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 Q9EPK5
- Elsewhere: RCSB PDB 5GN0 · PDBe 5GN0 · UniProt Q62296 · UniProt Q9EPK5
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