Crystal structure of the human eIF4A1/AMPPNP/amidino-rocaglate/polypurine RNA complex. Determined by X-ray diffraction at 1.69 Å resolution. Released 12 Mar 2025.
Explore 9DTS in 3D Show helices and sheets RCSB PDB PDBe
9DTS contains 86 α-helices and 56 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 | 34-36 | 3 | |
| α-helix | 41-50 | 10 | |
| α-helix | 57-67 | 11 | |
| β-strand | 72-75 | 4 | 1 |
| α-helix | 82-93 | 12 | |
| β-strand | 103-106 | 4 | 1 |
| α-helix | 110-123 | 14 | |
| β-strand | 131-134 | 4 | 1 |
| α-helix | 140-149 | 10 | |
| β-strand | 154-157 | 4 | 1 |
| α-helix | 159-167 | 9 | |
| β-strand | 178-182 | 5 | 1 |
| α-helix | 184-187 | 4 | |
| α-helix | 190-200 | 11 | |
| β-strand | 208-213 | 6 | 1 |
| α-helix | 218-224 | 7 | |
| β-strand | 232-234 | 3 | 1 |
| α-helix | 238-240 | 3 | |
| β-strand | 246-254 | 9 | 2 |
| α-helix | 256-258 | 3 | |
| α-helix | 259-269 | 11 | |
| β-strand | 274-278 | 5 | 2 |
| α-helix | 282-294 | 13 | |
| β-strand | 300-302 | 3 | 2 |
| α-helix | 308-320 | 13 | |
| β-strand | 325-328 | 4 | 2 |
| α-helix | 330-332 | 3 | |
| β-strand | 341-346 | 6 | 2 |
| α-helix | 349-350 | 2 | |
| α-helix | 353-360 | 8 | |
| α-helix | 365-367 | 3 | |
| β-strand | 370-377 | 8 | 2 |
| α-helix | 380-391 | 12 | |
| β-strand | 396-397 | 2 | 2 |
| α-helix | 398-399 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-36 | 3 | |
| α-helix | 41-50 | 10 | |
| α-helix | 57-67 | 11 | |
| β-strand | 72-75 | 4 | 3 |
| α-helix | 82-93 | 12 | |
| β-strand | 103-106 | 4 | 3 |
| α-helix | 110-123 | 14 | |
| β-strand | 131-134 | 4 | 3 |
| α-helix | 140-149 | 10 | |
| β-strand | 154-157 | 4 | 3 |
| α-helix | 159-167 | 9 | |
| β-strand | 178-181 | 4 | 3 |
| α-helix | 184-187 | 4 | |
| α-helix | 193-200 | 8 | |
| β-strand | 208-213 | 6 | 3 |
| α-helix | 218-223 | 6 | |
| α-helix | 224-226 | 3 | |
| β-strand | 232-234 | 3 | 3 |
| α-helix | 238-240 | 3 | |
| β-strand | 246-254 | 9 | 4 |
| α-helix | 256-258 | 3 | |
| α-helix | 259-269 | 11 | |
| β-strand | 274-278 | 5 | 4 |
| α-helix | 282-294 | 13 | |
| β-strand | 300-302 | 3 | 4 |
| α-helix | 308-320 | 13 | |
| β-strand | 325-328 | 4 | 4 |
| α-helix | 330-332 | 3 | |
| β-strand | 341-346 | 6 | 4 |
| α-helix | 349-350 | 2 | |
| α-helix | 353-360 | 8 | |
| α-helix | 365-367 | 3 | |
| β-strand | 370-377 | 8 | 4 |
| α-helix | 381-390 | 10 | |
| β-strand | 396-397 | 2 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-36 | 3 | |
| α-helix | 41-50 | 10 | |
| α-helix | 57-67 | 11 | |
| β-strand | 72-75 | 4 | 5 |
| α-helix | 82-93 | 12 | |
| β-strand | 103-106 | 4 | 5 |
| α-helix | 110-123 | 14 | |
| β-strand | 131-134 | 4 | 5 |
| α-helix | 140-149 | 10 | |
| β-strand | 154-157 | 4 | 5 |
| α-helix | 159-167 | 9 | |
| β-strand | 178-182 | 5 | 5 |
| α-helix | 184-187 | 4 | |
| α-helix | 190-200 | 11 | |
| β-strand | 208-213 | 6 | 5 |
| α-helix | 218-224 | 7 | |
| β-strand | 232-234 | 3 | 5 |
| α-helix | 238-240 | 3 | |
| β-strand | 246-252 | 7 | 6 |
| α-helix | 256-258 | 3 | |
| α-helix | 259-270 | 12 | |
| β-strand | 274-278 | 5 | 6 |
| α-helix | 282-294 | 13 | |
| β-strand | 300-302 | 3 | 6 |
| α-helix | 308-319 | 12 | |
| β-strand | 325-328 | 4 | 6 |
| α-helix | 330-332 | 3 | |
| β-strand | 341-346 | 6 | 6 |
| α-helix | 349-350 | 2 | |
| α-helix | 353-360 | 8 | |
| α-helix | 365-367 | 3 | |
| β-strand | 370-376 | 7 | 6 |
| α-helix | 378-391 | 14 | |
| β-strand | 396-397 | 2 | 6 |
| α-helix | 398 | 1 | |
| α-helix | 402-404 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-36 | 3 | |
| α-helix | 41-50 | 10 | |
| α-helix | 57-68 | 12 | |
| β-strand | 72-75 | 4 | 7 |
| α-helix | 82-93 | 12 | |
| β-strand | 103-106 | 4 | 7 |
| α-helix | 110-123 | 14 | |
| α-helix | 125-127 | 3 | |
| β-strand | 131-134 | 4 | 7 |
| α-helix | 140-149 | 10 | |
| β-strand | 154-157 | 4 | 7 |
| α-helix | 159-167 | 9 | |
| β-strand | 178-182 | 5 | 7 |
| α-helix | 184-187 | 4 | |
| α-helix | 190-200 | 11 | |
| β-strand | 208-213 | 6 | 7 |
| α-helix | 218-223 | 6 | |
| α-helix | 224-226 | 3 | |
| β-strand | 232-234 | 3 | 7 |
| α-helix | 238-240 | 3 | |
| β-strand | 246-252 | 7 | 8 |
| α-helix | 259-270 | 12 | |
| β-strand | 274-278 | 5 | 8 |
| α-helix | 282-294 | 13 | |
| β-strand | 300-302 | 3 | 8 |
| α-helix | 308-320 | 13 | |
| β-strand | 325-328 | 4 | 8 |
| α-helix | 330-332 | 3 | |
| β-strand | 341-346 | 6 | 8 |
| α-helix | 349-350 | 2 | |
| α-helix | 354-360 | 7 | |
| α-helix | 361-363 | 3 | |
| β-strand | 370-376 | 7 | 8 |
| α-helix | 381-391 | 11 | |
| β-strand | 396-397 | 2 | 8 |
| α-helix | 398 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic initiation factor 4A-I | A, B, C, D | protein | 388 | Homo sapiens | P60842 (AlphaFold model) |
| RNA (5'-r(p*ap*gp*ap*gp*ap*gp*ap*g)-3') | W, X, Y, Z | RNA | 10 | Homo sapiens |
>9DTS_1 Eukaryotic initiation factor 4A-I (chains A, B, C, D) SSGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQS GTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGT NVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYD IFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEW KLDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREF RSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTE EDKRTLRDIETFYNTSIEEMPLNVADLI
>9DTS_2 RNA (5'-R(P*AP*GP*AP*GP*AP*GP*AP*G)-3') (chains W, X, Y, Z) AGAGAGAGAG
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1BB1 | (3aR,4R,5S,5aR,10bR)-3a-hydroxy-N,8,10-trimethoxy-5a-(4-methoxyphenyl)-N,2-dime… | C31 H33 N3 O7 | 4 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 4 |
| MG | Magnesium ion | Mg | 4 |
Structural Basis for the Improved RNA Clamping of Amidino-Rocaglates to eIF4A1. Conley, J.F., Brown, L.E., McNeely, J.H. et al. ACS Omega (2025) 10:5795-5808. DOI 10.1021/acsomega.4c09421 · PubMed
Other PDB entries of the same protein (UniProt P60842 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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