MolNFT v1 · #116838 · protein
Crystal structure of human transcription factor TEAD2 in complex with flufenamic acid
5DQ8 · Transcriptional enhancer factor tef-4: “Crystal structure of human transcription factor TEAD2 in complex with flufenamic acid”. X-ray diffraction, 1 ligand (FLF), 6 pockets (best druggability 0.86). MolNFT v1 #116838 on GenesisL1…
- PDB
- 5DQ8
- Type
- protein
- Length
- 401 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional enhancer factor tef-4
- UniProt
- Q15562
- Ligands
- FLF
- Pockets
- 6 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional enhancer factor tef-4 | protein | 193 | 19% helix, 52% strand | Q15562 |
| B | Transcriptional enhancer factor tef-4 | protein | 208 | 17% helix, 49% strand | Q15562 |
Ligands and binding sites
- FLF · 2-[[3-(trifluoromethyl)phenyl]amino] benzoic acid · ligand · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.86 | 0.95 | 38 | FLF |
| 2 | 635 | 0.78 | 0.83 | 67 | FLF |
| 3 | 334 | 0.70 | 0.83 | 39 | empty |
| 4 | 53 | 0.36 | 0.79 | 12 | empty |
| 5 | 72 | 0.33 | 0.74 | 18 | FLF |
Interfaces
1 interface between chains.
- A–B · 752 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5DQ8 · Crystal structure of human transcription factor TEAD2 in complex with flufenamic acid · 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 5DQ8 · PDBe 5DQ8 · UniProt Q15562
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