Crystal Structure of eIF4E Bound to Glycerol and eIF4G1 peptide. Determined by X-ray diffraction at 2.29 Å resolution. Released 31 Mar 2010.
Explore 2W97 in 3D Show helices and sheets RCSB PDB PDBe
2W97 contains 23 α-helices and 16 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 | |
| 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 | 200-204 | 5 | |
| α-helix | 212-213 | 2 | |
| β-strand | 215-216 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-33 | 3 | |
| β-strand | 38-49 | 12 | 2 |
| β-strand | 60-68 | 9 | 2 |
| α-helix | 69-78 | 10 | |
| α-helix | 82-84 | 3 | |
| α-helix | 86 | 1 | |
| β-strand | 89-95 | 7 | 2 |
| β-strand | 111-116 | 6 | 2 |
| 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 | 2 |
| β-strand | 162-167 | 6 | 2 |
| α-helix | 173-186 | 14 | |
| β-strand | 196-199 | 4 | 2 |
| α-helix | 200-205 | 6 | |
| β-strand | 215-216 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 626-631 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 626-630 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic translation initiation factor 4E | A | protein | 217 | HOMO SAPIENS | P06730 (AlphaFold model) |
| Eukaryotic translation initiation factor 4E | B | protein | 217 | HOMO SAPIENS | P06730 (AlphaFold model) |
| Eukaryotic translation initiation factor 4 gamma 1 | E, F | protein | 14 | HOMO SAPIENS | Q04637 (AlphaFold model) |
>2W97_1 EUKARYOTIC TRANSLATION INITIATION FACTOR 4E (chains A) MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANL RLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQ QRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIG RVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
>2W97_2 EUKARYOTIC TRANSLATION INITIATION FACTOR 4E (chains B) MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKKDKSKTWQANL RLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQ QRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIG RVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
>2W97_3 EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1 (chains E, F) KKRYDREFLLGFQF
| ID | Name | Formula | Copies |
|---|---|---|---|
| MGO | [[(2R,3S,4R,5R)-5-(6-amino-3-methyl-4-oxo-5H-IMIDAZO[4,5-c]pyridin-1-yl)-3,4-di… | C12 H20 N4 O14 P3 | 1 |
Water and common crystallization additives (GOL, SO4, PGE) are not listed.
Crystallization of eIF4E complexed with eIF4GI peptide and glycerol reveals distinct structural differences around the cap-binding site. Brown, C.J., Verma, C.S., Walkinshaw, M.D. et al. Cell Cycle (2009) 8:1905-1911. DOI 10.4161/cc.8.12.8742 · 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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