Translation initiation factor 4E in complex with m7GppppG mRNA 5' cap analog. Determined by X-ray diffraction at 1.87 Å resolution. Released 10 May 2017.
Explore 5J5O in 3D Show helices and sheets RCSB PDB PDBe
5J5O contains 40 α-helices and 35 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 | 57-59 | 3 | |
| β-strand | 60-68 | 9 | 1 |
| α-helix | 69-76 | 8 | |
| β-strand | 79 | 1 | 2 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-95 | 6 | 1 |
| β-strand | 111-116 | 6 | 1 |
| α-helix | 121 | 1 | |
| 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 | 173-186 | 14 | |
| β-strand | 196-199 | 4 | 1 |
| α-helix | 200-203 | 4 | |
| β-strand | 215-216 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 38-48 | 11 | 3 |
| 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 | 121 | 1 | |
| 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 | 200-203 | 4 | |
| β-strand | 215-216 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 35 | 1 | 2 |
| β-strand | 38-48 | 11 | 5 |
| α-helix | 56-59 | 4 | |
| β-strand | 60-68 | 9 | 5 |
| α-helix | 69-78 | 10 | |
| α-helix | 82-84 | 3 | |
| α-helix | 86 | 1 | |
| β-strand | 89-95 | 7 | 5 |
| β-strand | 111-116 | 6 | 5 |
| α-helix | 121 | 1 | |
| α-helix | 122-126 | 5 | |
| α-helix | 127-138 | 12 | |
| α-helix | 143-148 | 6 | |
| β-strand | 149-156 | 8 | 5 |
| β-strand | 162-167 | 6 | 5 |
| α-helix | 173-187 | 15 | |
| β-strand | 196-199 | 4 | 5 |
| α-helix | 200-202 | 3 | |
| β-strand | 215-216 | 2 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 35 | 1 | 4 |
| α-helix | 36-37 | 2 | |
| β-strand | 38-48 | 11 | 6 |
| α-helix | 57-59 | 3 | |
| β-strand | 60-68 | 9 | 6 |
| α-helix | 69-78 | 10 | |
| α-helix | 82-84 | 3 | |
| α-helix | 86 | 1 | |
| β-strand | 89-95 | 7 | 6 |
| α-helix | 105-108 | 4 | |
| β-strand | 111-116 | 6 | 6 |
| α-helix | 121 | 1 | |
| α-helix | 122-126 | 5 | |
| α-helix | 127-138 | 12 | |
| α-helix | 143-148 | 6 | |
| β-strand | 149-156 | 8 | 6 |
| β-strand | 162-167 | 6 | 6 |
| α-helix | 173-187 | 15 | |
| β-strand | 198-199 | 2 | 6 |
| α-helix | 200-203 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic translation initiation factor 4E | A, B, C, D | protein | 190 | Mus musculus | P63073 (AlphaFold model) |
>5J5O_1 Eukaryotic translation initiation factor 4E (chains A, B, C, D) VANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMP GCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSD DVCGAVVNVRAKGDKIAIWTTECENRDAVTHIGRVYKERLGLPPKIVIGYQSHADTATKS GSTTKNRFVV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6G0 | 5'-O-[(R)-hydroxy{[(R)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}phospho… | C11 H20 N5 O17 P4 | 4 |
Water and common crystallization additives (GOL) are not listed.
mRNA cap analogues substituted in the tetraphosphate chain with CX2: identification of O-to-CCl2 as the first bridging modification that confers resistance to decapping without impairing translation. Rydzik, A.M., Warminski, M., Sikorski, P.J. et al. Nucleic Acids Res (2017) 45:8661-8675. DOI 10.1093/nar/gkx569 · PubMed
Other PDB entries of the same protein (UniProt P63073 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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