MolNFT v1 · #145095 · protein
Crystal structure of tead complexed with its inhibitor
6CDY · Transcriptional enhancer factor tef-4: “Crystal structure of tead complexed with its inhibitor”. X-ray diffraction, 1 ligand (EY1), 5 pockets (best druggability 0.85). MolNFT v1 #145095 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6CDY
- Type
- protein
- Length
- 400 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional enhancer factor tef-4
- UniProt
- Q15562
- Ligands
- EY1
- Pockets
- 5 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional enhancer factor tef-4 | protein | 193 | 18% helix, 52% strand | Q15562 |
| B | Transcriptional enhancer factor tef-4 | protein | 207 | 19% helix, 49% strand | Q15562 |
Ligands and binding sites
- EY1 · 2-[(4H-1,2,4-triazol-3-yl)sulfanyl]-N-{4-[(3s,5s,7s)-tricyclo[3.3.1.1~3,7~]decan-1-yl]phenyl}acetamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.85 | 0.96 | 32 | EY1 |
| 2 | 754 | 0.77 | 0.81 | 84 | EY1 |
| 3 | 316 | 0.67 | 0.82 | 35 | empty |
| 4 | 61 | 0.34 | 0.77 | 10 | empty |
| 5 | 56 | 0.30 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 690 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6CDY · Crystal structure of TEAD complexed with its inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- Q15562 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-4 (Q15562) · 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 Q15562
- Elsewhere: RCSB PDB 6CDY · PDBe 6CDY · UniProt Q15562
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