1EJH: EIF4E/EIF4G PEPTIDE/7-methyl-GDP
EIF4E/EIF4G PEPTIDE/7-methyl-GDP. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Mar 2000.
- Method
- X-ray diffraction
- Resolution
- 2.2 Å
- Organism
- Mus musculus
- Chains
- 8
- Atoms
- 6,481
- Mol. weight
- 98.61 kDa
- Ligands
- M7G
- Released
- 10 Mar 2000
Explore 1EJH in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1EJH contains 39 α-helices and 33 β-strands across 8 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.
Chain A: 7 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 38-48 | 11 | 1 |
| β-strand | 60-68 | 9 | 1 |
| α-helix | 69-76 | 8 | |
| α-helix | 82-84 | 3 | |
| α-helix | 86 | 1 | |
| β-strand | 89-95 | 7 | 1 |
| β-strand | 111-117 | 7 | 1 |
| α-helix | 125-138 | 14 | |
| α-helix | 143-148 | 6 | |
| β-strand | 149-156 | 8 | 1 |
| β-strand | 161-167 | 7 | 1 |
| α-helix | 173-186 | 14 | |
| β-strand | 196-199 | 4 | 1 |
| α-helix | 200-204 | 5 | |
| β-strand | 215-216 | 2 | 1 |
Chain B: 12 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 34-36 | 3 | |
| β-strand | 38-48 | 11 | 2 |
| β-strand | 54 | 1 | 3 |
| α-helix | 56-59 | 4 | |
| β-strand | 60-68 | 9 | 2 |
| α-helix | 69-76 | 8 | |
| α-helix | 82-84 | 3 | |
| α-helix | 86 | 1 | |
| β-strand | 90-95 | 6 | 2 |
| α-helix | 105-108 | 4 | |
| β-strand | 111-116 | 6 | 2 |
| α-helix | 121 | 1 | |
| α-helix | 122-126 | 5 | |
| α-helix | 127-138 | 12 | |
| α-helix | 143-148 | 6 | |
| β-strand | 149-155 | 7 | 2 |
| β-strand | 162-167 | 6 | 2 |
| α-helix | 173-187 | 15 | |
| β-strand | 196-199 | 4 | 2 |
| α-helix | 200-203 | 4 | |
| β-strand | 215-216 | 2 | 2 |
Chain C: 10 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 34-36 | 3 | |
| β-strand | 38-48 | 11 | 4 |
| α-helix | 56-59 | 4 | |
| β-strand | 60-68 | 9 | 4 |
| α-helix | 69-78 | 10 | |
| α-helix | 80-81 | 2 | |
| α-helix | 82-84 | 3 | |
| β-strand | 90-95 | 6 | 4 |
| β-strand | 111-117 | 7 | 4 |
| α-helix | 119-122 | 4 | |
| α-helix | 126-138 | 13 | |
| α-helix | 143-145 | 3 | |
| β-strand | 149-155 | 7 | 4 |
| β-strand | 161-167 | 7 | 4 |
| α-helix | 173-187 | 15 | |
| β-strand | 196-199 | 4 | 4 |
| α-helix | 200-204 | 5 | |
| β-strand | 215-216 | 2 | 4 |
Chain D: 6 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 38-48 | 11 | 3 |
| α-helix | 56-59 | 4 | |
| β-strand | 60-68 | 9 | 3 |
| α-helix | 69-77 | 9 | |
| α-helix | 82-84 | 3 | |
| β-strand | 90-95 | 6 | 3 |
| β-strand | 111-116 | 6 | 3 |
| α-helix | 126-139 | 14 | |
| α-helix | 143-148 | 6 | |
| β-strand | 149-155 | 7 | 3 |
| β-strand | 162-167 | 6 | 3 |
| α-helix | 173-186 | 14 | |
| β-strand | 196-199 | 4 | 3 |
| β-strand | 215-216 | 2 | 3 |
Chains E and H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 626-630 | 5 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 626-631 | 6 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 626-632 | 7 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Eukaryotic initiation factor 4E | A, B, C, D | protein | 190 | Mus musculus | P63073 (AlphaFold model) |
| Eukaryotic initiation factor 4GII | E, F, G, H | protein | 16 | | Q13541 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>1EJH_1 EUKARYOTIC INITIATION FACTOR 4E (chains A, B, C, D)
VANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMP
GCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSD
DVCGAVVNVRAKGDKIAIWTTECENRDAVTHIGRVYKERLGLPPKIVIGYQSHADTATKS
GSTTKNRFVV
Sequence of entity 2 (E, F, G, H), FASTA
>1EJH_2 EUKARYOTIC INITIATION FACTOR 4GII (chains E, F, G, H)
KQYDREFLLDFQFMPA
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| M7G | 7N-methyl-8-hydroguanosine-5'-diphosphate | C11 H18 N5 O11 P2 | 4 |
Primary citation
Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Marcotrigiano, J., Gingras, A.C., Sonenberg, N. et al. Mol Cell (1999) 3:707-716. DOI 10.1016/S1097-2765(01)80003-4 · PubMed
Other PDB entries of the same protein (UniProt P63073 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5M7X 1.68 Å, Translation initiation factor 4E in complex with (RP)-m2(7,2'O)GppSepG mRNA 5' cap…
- 5M7Z 1.69 Å, Translation initiation factor 4E in complex with (SP)-m2(7,2'O)GppSepG mRNA 5' cap…
- 5M7V 1.74 Å, Translation initiation factor 4E in complex with (RP)-m2(7,2'O)GppSpG mRNA 5' cap analog…
- 5J5Y 1.75 Å, Translation initiation factor 4E in complex with m2(7,2'O)GppCCl2ppG mRNA 5' cap analog
- 6U09 1.79 Å, Discovery of Lysine-Targeted eIF4E Inhibitors through Covalent Docking
- 1L8B 1.8 Å, Cocrystal Structure of the Messenger RNA 5' Cap-binding Protein (eIF4E) bound to…
- 5M84 1.85 Å, Translation initiation factor 4E in complex with (SP)-m2(7,2'O)GppSpA mRNA 5' cap analog
- 6GKK 1.86 Å, Translation initiation factor 4E in complex with beta-phosphorothioate trinucleotide…
- 5M83 1.86 Å, Translation initiation factor 4E in complex with (RP)-m2(7,2'O)GppSpA mRNA 5' cap analog
- 5J5O 1.87 Å, Translation initiation factor 4E in complex with m7GppppG mRNA 5' cap analog
- 5M81 1.9 Å, Translation initiation factor 4E in complex with (SP)-iPr-m7GppSpG mRNA 5' cap analog
- 5OSX 1.92 Å, Translation initiation factor 4E in complex with m7G(5'S)ppp(5'S)G mRNA 5' cap analog
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