Research workbench
Cocrystal structure of EIF4E/4E-BP1 peptide
Analyse Cocrystal structure of EIF4E/4E-BP1 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EJ4
- Type
- protein
- Length
- 193 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eukaryotic initiation factor 4E; Eukaryotic translation initiation factor 4E binding…
- UniProt
- P63073
- Ligands
- M7G
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eukaryotic initiation factor 4E | protein | 179 | 35% helix, 32% strand | P63073 |
| B | Eukaryotic translation initiation factor 4E binding protein 1 | protein | 14 | 43% helix, 0% strand | — |
Ligands and binding sites
- M7G · 7N-methyl-8-hydroguanosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.52 | 0.81 | 22 | M7G |
Interfaces
1 interface between chains.
- A–B · 672 Ų buried · 11 hydrogen bonds · protein-protein
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 P63073
- Elsewhere: RCSB PDB 1EJ4 · PDBe 1EJ4 · UniProt P63073
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