Research workbench
Crystal structure of the E2F4-DP1 coiled coil and marked-box domains
Analyse Crystal structure of the E2F4-DP1 coiled coil and marked-box domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TUU
- Type
- protein
- Length
- 250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription factor DP1; Transcription factor E2F4
- UniProt
- Q14186, Q16254
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription factor DP1 | protein | 144 | 56% helix, 17% strand | Q14186 |
| B | Transcription factor E2F4 | protein | 106 | 42% helix, 22% strand | Q16254 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.33 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 3096 Ų buried · 51 hydrogen bonds · protein-protein
Compared structures
- 5TUU · Crystal structure of the E2F4-DP1 coiled coil and marked-box domains · the same entry in another collection · chain A against A, TM-score 1.00
- Q16254 · AlphaFold monomer V2.0 prediction for transcription factor E2F4 (Q16254) · a predicted model of the same protein · chain B against A, TM-score 0.95
- Q14186 · AlphaFold monomer V2.0 prediction for transcription factor dp-1 (Q14186) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q14186
- Every structure of UniProt Q16254
- Elsewhere: RCSB PDB 5TUU · PDBe 5TUU · UniProt Q14186 · UniProt Q16254
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