MolNFT v1 · #126812 · protein
Crystal structure of EIF4E from C. melo bound to a EIF4G peptide
5ME5 · Eukaryotic transcription initiation factor 4E: “Crystal structure of EIF4E from C. melo bound to a EIF4G peptide”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #126812 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5ME5
- Type
- protein
- Length
- 189 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eukaryotic transcription initiation factor 4E; EIF4G
- UniProt
- Q00LS8
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eukaryotic transcription initiation factor 4E | protein | 152 | 30% helix, 37% strand | Q00LS8 |
| B | EIF4G | protein | 37 | 41% helix, 3% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1444 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5ME5 · Crystal Structure of eiF4E from C. melo bound to a eIF4G peptide · the same entry in another collection · chain A against A, TM-score 1.00
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 Q00LS8
- Elsewhere: RCSB PDB 5ME5 · PDBe 5ME5 · UniProt Q00LS8
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