Research workbench
Crystal structure of EIF4E in complex with a stapled peptide derivative
Analyse Crystal structure of EIF4E in complex with a stapled peptide derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BEA
- Type
- protein
- Length
- 193 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eukaryotic translation initiation factor 4E; Stapled EIF4E interacting peptide
- UniProt
- P06730
- Ligands
- NME
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eukaryotic translation initiation factor 4E | protein | 181 | 34% helix, 28% strand | P06730 |
| B | Stapled EIF4E interacting peptide | protein | 12 | 50% helix, 0% strand | — |
Ligands and binding sites
- NME · Methylamine · ion · chains A, B
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 | 173 | 0.47 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 605 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 4BEA · Crystal Structure of eIF4E in Complex with a Stapled Peptide Derivative · the same entry in another collection · chain A against A, TM-score 1.00
- P06730 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 4E (P06730) · 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 P06730
- Elsewhere: RCSB PDB 4BEA · PDBe 4BEA · UniProt P06730
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