Research workbench
Human TEAD2 transcriptional factor
Analyse Human TEAD2 transcriptional factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3L15
- Type
- protein
- Length
- 397 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional enhancer factor tef-4
- UniProt
- Q15562
- Pockets
- 4 · 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 | 204 | 20% helix, 50% strand | Q15562 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains 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 | 244 | 0.85 | 0.96 | 37 | empty |
| 2 | 872 | 0.80 | 0.83 | 101 | GOL |
| 3 | 83 | 0.37 | 0.76 | 14 | empty |
| 4 | 75 | 0.37 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 724 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
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 3L15 · PDBe 3L15 · UniProt Q15562
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