Translation initiation factor 4E in complex with m2(7,2'O)GppCCl2ppG mRNA 5' cap analog. Determined by X-ray diffraction at 1.75 Å resolution. Released 10 May 2017.
Explore 5J5Y in 3D Show helices and sheets RCSB PDB PDBe
5J5Y contains 36 α-helices and 33 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 | 69-78 | 10 | |
| 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 | 121-124 | 4 | |
| α-helix | 126-138 | 13 | |
| 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 |
|---|---|---|---|
| α-helix | 35-37 | 3 | |
| β-strand | 38-48 | 11 | 3 |
| α-helix | 57-59 | 3 | |
| β-strand | 60-68 | 9 | 3 |
| α-helix | 69-78 | 10 | |
| 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 | 121-124 | 4 | |
| α-helix | 126-138 | 13 | |
| 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 |
| 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 | |
| β-strand | 89-95 | 7 | 5 |
| α-helix | 105-107 | 3 | |
| β-strand | 111-117 | 7 | 5 |
| α-helix | 121 | 1 | |
| α-helix | 122-126 | 5 | |
| α-helix | 127-138 | 12 | |
| β-strand | 149-156 | 8 | 5 |
| β-strand | 161-167 | 7 | 5 |
| α-helix | 178-186 | 9 |
| 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 | |
| β-strand | 90-95 | 6 | 6 |
| β-strand | 112-116 | 5 | 6 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| α-helix | 127-138 | 12 | |
| α-helix | 143-145 | 3 | |
| β-strand | 151-155 | 5 | 6 |
| β-strand | 162-166 | 5 | 6 |
| α-helix | 174-187 | 14 | |
| β-strand | 198 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic translation initiation factor 4E | A, B, C, D | protein | 190 | Mus musculus | P63073 (AlphaFold model) |
>5J5Y_1 Eukaryotic translation initiation factor 4E (chains A, B, C, D) VANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMP GCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSD DVCGAVVNVRAKGDKIAIWTTECENRDAVTHIGRVYKERLGLPPKIVIGYQSHADTATKS GSTTKNRFVV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6G6 | 2-amino-9-{5-O-[(R)-{[(S)-{dichloro[(R)-hydroxy(phosphonooxy)phosphoryl]methyl}… | C13 H21 Cl2 N5 O16 P4 | 2 |
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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