MolNFT v1 · #167092 · protein
Crystal structure of human TEAD2 transcription factor in complex with flufenamic acid derivative
6VAH · Transcriptional enhancer factor tef-4: “Crystal structure of human TEAD2 transcription factor in complex with flufenamic acid derivative”. X-ray diffraction, 2 ligands (QZ1, UNX), 4 pockets (best druggability 0.84). MolNFT v1…
- PDB
- 6VAH
- Type
- protein
- Length
- 403 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional enhancer factor tef-4
- UniProt
- Q15562
- Ligands
- QZ1, UNX
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional enhancer factor tef-4 | protein | 208 | 19% helix, 49% strand | Q15562 |
| B | Transcriptional enhancer factor tef-4 | protein | 195 | 18% helix, 51% strand | Q15562 |
Ligands and binding sites
- QZ1 · 2-fluoro-6-[(3-hexylphenyl)amino]benzoic acid · ligand · 2 copies · chains A, B
- UNX · Unknown atom or ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 559 | 0.84 | 0.89 | 56 | QZ1 |
| 2 | 430 | 0.77 | 0.86 | 63 | QZ1 |
| 3 | 85 | 0.33 | 0.74 | 17 | empty |
| 4 | 62 | 0.33 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 589 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6VAH · Crystal structure of human TEAD2 transcription factor 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 B 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 6VAH · PDBe 6VAH · UniProt Q15562
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