Research workbench
Crystal structure of human transcription factor TEAD2 in complex with bromo-fenamic acid
Analyse Crystal structure of human transcription factor TEAD2 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DQE
- 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
- 5E4
- Pockets
- 4 · best druggability 0.86
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 | 193 | 19% helix, 52% strand | Q15562 |
| B | Transcriptional enhancer factor tef-4 | protein | 208 | 20% helix, 49% strand | Q15562 |
Ligands and binding sites
- 5E4 · 2-[(3-bromophenyl)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
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.86 | 0.96 | 38 | 5E4 |
| 2 | 704 | 0.78 | 0.83 | 75 | 5E4 |
| 3 | 250 | 0.67 | 0.84 | 34 | empty |
| 4 | 86 | 0.36 | 0.75 | 16 | 5E4 |
Interfaces
1 interface between chains.
- A–B · 789 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5DQE · Crystal structure of human transcription factor TEAD2 in complex with bromo-fenamic 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 5DQE · PDBe 5DQE · UniProt Q15562
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