eIF4E complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 15 Jul 2015.
Explore 5BXV in 3D Show helices and sheets RCSB PDB PDBe
5BXV contains 28 α-helices and 19 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 |
|---|---|---|---|
| α-helix | 35-37 | 3 | |
| 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 | |
| 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 | 127-139 | 13 | |
| 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 | 200-203 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 56-62 | 7 | |
| α-helix | 66-69 | 4 | |
| β-strand | 82 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 37 | 1 | |
| β-strand | 38-48 | 11 | 3 |
| α-helix | 57-59 | 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 | 200-204 | 5 | |
| α-helix | 211-213 | 3 | |
| β-strand | 215-216 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 56-61 | 6 | |
| α-helix | 62-64 | 3 | |
| α-helix | 66-69 | 4 | |
| β-strand | 82 | 1 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic translation initiation factor 4E | A, C | protein | 192 | Mus musculus | P63073 (AlphaFold model) |
| Eukaryotic translation initiation factor 4E-binding protein 1 | B, D | protein | 44 | Homo sapiens | Q13541 (AlphaFold model) |
>5BXV_1 Eukaryotic translation initiation factor 4E (chains A, C) GEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNL MPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDY SDDVCGAVVNVRAKGDKIAIWTTECENRDAVTHIGRVYKERLGLPPKIVIGYQSHADTAT KSGSTTKNRFVV
>5BXV_2 Eukaryotic translation initiation factor 4E-binding protein 1 (chains B, D) GEFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSP
| ID | Name | Formula | Copies |
|---|---|---|---|
| MGP | 7-methyl-guanosine-5'-triphosphate | C11 H19 N5 O14 P3 | 2 |
Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1. Sekiyama, N., Arthanari, H., Papadopoulos, E. et al. Proc Natl Acad Sci U S A (2015) 112:E4036-E4045. DOI 10.1073/pnas.1512118112 · 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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