Crystal structure of the human eIF4E-eIF4G complex. Determined by X-ray diffraction at 1.53 Å resolution. Released 26 Oct 2016.
Explore 5T46 in 3D Show helices and sheets RCSB PDB PDBe
5T46 contains 27 α-helices and 18 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 38-48 | 11 | 1 |
| α-helix | 56-59 | 4 | |
| β-strand | 60-68 | 9 | 1 |
| α-helix | 69-76 | 8 | |
| β-strand | 79 | 1 | 2 |
| α-helix | 82-84 | 3 | |
| α-helix | 86 | 1 | |
| β-strand | 90-95 | 6 | 1 |
| β-strand | 111-116 | 6 | 1 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| α-helix | 127-138 | 12 | |
| α-helix | 143-148 | 6 | |
| β-strand | 149-155 | 7 | 1 |
| β-strand | 162-167 | 6 | 1 |
| α-helix | 173-187 | 15 | |
| β-strand | 196-199 | 4 | 1 |
| α-helix | 200-205 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 614-618 | 5 | |
| α-helix | 624-627 | 4 | |
| α-helix | 629-630 | 2 | |
| β-strand | 640 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-33 | 3 | |
| β-strand | 38-48 | 11 | 3 |
| α-helix | 56-59 | 4 | |
| β-strand | 60-68 | 9 | 3 |
| α-helix | 69-76 | 8 | |
| β-strand | 79 | 1 | 4 |
| α-helix | 82-84 | 3 | |
| α-helix | 86 | 1 | |
| β-strand | 90-95 | 6 | 3 |
| β-strand | 111-116 | 6 | 3 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| α-helix | 127-138 | 12 | |
| α-helix | 143-148 | 6 | |
| β-strand | 149-155 | 7 | 3 |
| β-strand | 162-167 | 6 | 3 |
| α-helix | 173-187 | 15 | |
| β-strand | 196-199 | 4 | 3 |
| α-helix | 200-204 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic translation initiation factor 4E | A, C | protein | 220 | Homo sapiens | P06730 (AlphaFold model) |
| Eukaryotic translation initiation factor 4 gamma 1 | B, D | protein | 66 | Homo sapiens | Q04637 (AlphaFold model) |
>5T46_1 Eukaryotic translation initiation factor 4E (chains A, C) MLEMATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQ ANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITL NKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVT HIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
>5T46_2 Eukaryotic translation initiation factor 4 gamma 1 (chains B, D) GPHMQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKT PLRPLD
| ID | Name | Formula | Copies |
|---|---|---|---|
| MGP | 7-methyl-guanosine-5'-triphosphate | C11 H19 N5 O14 P3 | 2 |
Water and common crystallization additives (GOL) are not listed.
The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation. Gruner, S., Peter, D., Weber, R. et al. Mol Cell (2016) 64:467-479. DOI 10.1016/j.molcel.2016.09.020 · PubMed
Other PDB entries of the same protein (UniProt P06730 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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