MolNFT v2 · #120345 · protein
Structure of TAZ-TEAD complex
5GN0: “Structure of TAZ-TEAD complex”. X-ray diffraction at 2.9, 1 ligand (PLM). MolNFT v2 #120345 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- Q62296, Q9EPK5
- Ligands
- PLM
Structure
x-ray diffraction · resolution 2.9 · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 222 | — | Q62296 |
| D | — | protein | 221 | — | Q62296 |
| E, H | — | protein | 32 | — | Q9EPK5 |
| F | — | protein | 30 | — | Q9EPK5 |
| G | — | protein | 33 | — | 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.
Compared structures
- 5GN0 · Structure of taz-tead complex · the same entry in another collection · chain A against A, TM-score 1.00
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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