Crystal structure of apoform human eIF4A1 C-terminal domain. Determined by X-ray diffraction at 2.73 Å resolution. Released 18 Feb 2026.
Explore 9I9F in 3D Show helices and sheets RCSB PDB PDBe
9I9F contains 29 α-helices and 27 β-strands across 3 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 | 242 | 1 | 1 |
| β-strand | 246-252 | 7 | 2 |
| α-helix | 256-258 | 3 | |
| α-helix | 259-266 | 8 | |
| α-helix | 267-271 | 5 | |
| β-strand | 275-278 | 4 | 2 |
| α-helix | 282-294 | 13 | |
| β-strand | 300-301 | 2 | 2 |
| α-helix | 308-316 | 9 | |
| α-helix | 317-321 | 5 | |
| β-strand | 325-328 | 4 | 2 |
| α-helix | 332-335 | 4 | |
| α-helix | 338-340 | 3 | |
| β-strand | 343-346 | 4 | 2 |
| α-helix | 353-360 | 8 | |
| β-strand | 362 | 1 | 1 |
| β-strand | 370-376 | 7 | 2 |
| α-helix | 380-390 | 11 | |
| β-strand | 396-397 | 2 | 2 |
| α-helix | 398 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 242 | 1 | 3 |
| β-strand | 247-252 | 6 | 4 |
| α-helix | 256-258 | 3 | |
| α-helix | 259-269 | 11 | |
| β-strand | 275-278 | 4 | 4 |
| α-helix | 282-294 | 13 | |
| β-strand | 300-301 | 2 | 4 |
| α-helix | 308-319 | 12 | |
| β-strand | 325-328 | 4 | 4 |
| α-helix | 330-334 | 5 | |
| α-helix | 338-340 | 3 | |
| β-strand | 343-346 | 4 | 4 |
| α-helix | 354-360 | 7 | |
| β-strand | 362 | 1 | 3 |
| β-strand | 371-376 | 6 | 4 |
| α-helix | 378-390 | 13 | |
| β-strand | 396-397 | 2 | 4 |
| α-helix | 398 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 242 | 1 | 5 |
| β-strand | 246-252 | 7 | 6 |
| α-helix | 256-258 | 3 | |
| α-helix | 259-269 | 11 | |
| β-strand | 275-278 | 4 | 6 |
| α-helix | 282-294 | 13 | |
| β-strand | 300-301 | 2 | 6 |
| α-helix | 308-319 | 12 | |
| β-strand | 325-328 | 4 | 6 |
| α-helix | 330-334 | 5 | |
| α-helix | 338-340 | 3 | |
| β-strand | 343-346 | 4 | 6 |
| α-helix | 354-360 | 7 | |
| β-strand | 362 | 1 | 5 |
| β-strand | 370-376 | 7 | 6 |
| α-helix | 378-390 | 13 | |
| β-strand | 396-397 | 2 | 6 |
| α-helix | 398 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic initiation factor 4A-I | A, B, C | protein | 170 | Homo sapiens | P60842 (AlphaFold model) |
>9I9F_1 Eukaryotic initiation factor 4A-I (chains A, B, C) GSEELTLEGIRQFYINVEREEWKLDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARD FTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENY IHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI
The mechanism of selective eIF4A1-dependent translation. Schmidt, T., Turnbull, A.P., Bushell, M. To be published.
Other PDB entries of the same protein (UniProt P60842 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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