Research workbench
Complex of D. melanogaster EIF4E with the 4E-binding protein 4E-T
Analyse Complex of D. melanogaster EIF4E with the 4E-binding protein 4E-T in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UE9
- Type
- protein
- Length
- 210 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eukaryotic translation initiation factor 4E; Eukaryotic translation initiation factor 4E…
- UniProt
- P48598, Q8IH18
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eukaryotic translation initiation factor 4E | protein | 174 | 26% helix, 32% strand | P48598 |
| B | Eukaryotic translation initiation factor 4E transporter | protein | 36 | 17% helix, 3% strand | Q8IH18 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.44 | 0.75 | 29 | empty |
| 2 | 51 | 0.26 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1430 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 4UE9 · Complex of D. melanogaster eIF4E with the 4E-binding protein 4E-T · the same entry in another collection · chain A against A, TM-score 1.00
- P48598 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 4E1… · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q8IH18 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 4E… · a predicted model of the same protein · chain B against A, TM-score 0.44
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 P48598
- Every structure of UniProt Q8IH18
- Elsewhere: RCSB PDB 4UE9 · PDBe 4UE9 · UniProt P48598 · UniProt Q8IH18
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