Research workbench
Structure of EIF4E-cup complex
Analyse Structure of EIF4E-cup complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AXG
- Type
- protein
- Length
- 400 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P48598, Q9VMA3
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 181 | — | P48598 |
| B | — | protein | 167 | — | P48598 |
| C | — | protein | 37 | — | Q9VMA3 |
| D | — | protein | 15 | — | Q9VMA3 |
Compared structures
- 4AXG · Structure of eIF4E-Cup complex · the same entry in another collection · chain D against D, TM-score 1.00
- P48598 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 4E1… · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q9VMA3 · AlphaFold monomer V2.0 prediction for protein cup (Q9VMA3) · a predicted model of the same protein · chain C against A, TM-score 0.90
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 Q9VMA3
- Elsewhere: RCSB PDB 4AXG · PDBe 4AXG · UniProt P48598 · UniProt Q9VMA3
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