Crystal structure of Pdcd4-eIF4A. Determined by X-ray diffraction at 3.5 Å resolution. Released 24 Feb 2009.
Explore 3EIQ in 3D Show helices and sheets RCSB PDB PDBe
3EIQ contains 59 α-helices and 28 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 |
|---|---|---|---|
| α-helix | 23-25 | 3 | |
| α-helix | 34-37 | 4 | |
| α-helix | 41-49 | 9 | |
| α-helix | 57-67 | 11 | |
| β-strand | 72-74 | 3 | 1 |
| α-helix | 77 | 1 | |
| α-helix | 79 | 1 | |
| α-helix | 83-93 | 11 | |
| β-strand | 103-106 | 4 | 1 |
| α-helix | 110-123 | 14 | |
| α-helix | 124-126 | 3 | |
| β-strand | 131-133 | 3 | 1 |
| α-helix | 140-147 | 8 | |
| β-strand | 154-157 | 4 | 1 |
| α-helix | 159-168 | 10 | |
| β-strand | 178-181 | 4 | 1 |
| α-helix | 184-187 | 4 | |
| α-helix | 188-192 | 5 | |
| α-helix | 193-200 | 8 | |
| β-strand | 208-212 | 5 | 1 |
| α-helix | 218-224 | 7 | |
| β-strand | 232-234 | 3 | 1 |
| β-strand | 248-252 | 5 | 2 |
| α-helix | 259-268 | 10 | |
| β-strand | 276-278 | 3 | 2 |
| α-helix | 282-293 | 12 | |
| β-strand | 300-301 | 2 | 2 |
| α-helix | 307-318 | 12 | |
| β-strand | 326-328 | 3 | 2 |
| α-helix | 338-340 | 3 | |
| β-strand | 344-346 | 3 | 2 |
| α-helix | 354-359 | 6 | |
| β-strand | 372-376 | 5 | 2 |
| α-helix | 380-390 | 11 | |
| β-strand | 396-397 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 162-178 | 17 | |
| α-helix | 181-189 | 9 | |
| α-helix | 195-199 | 5 | |
| α-helix | 200-208 | 9 | |
| α-helix | 213-224 | 12 | |
| α-helix | 233-245 | 13 | |
| α-helix | 247-253 | 7 | |
| α-helix | 257-270 | 14 | |
| α-helix | 280-282 | 3 | |
| α-helix | 289-302 | 14 | |
| α-helix | 324-341 | 18 | |
| α-helix | 344-354 | 11 | |
| α-helix | 360-373 | 14 | |
| α-helix | 378-392 | 15 | |
| α-helix | 398-418 | 21 | |
| α-helix | 422-436 | 15 | |
| α-helix | 441-444 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-37 | 4 | |
| α-helix | 41-49 | 9 | |
| α-helix | 59-67 | 9 | |
| β-strand | 72-74 | 3 | 3 |
| α-helix | 79 | 1 | |
| α-helix | 83-93 | 11 | |
| β-strand | 103-106 | 4 | 3 |
| α-helix | 110-123 | 14 | |
| α-helix | 124-126 | 3 | |
| β-strand | 131-133 | 3 | 3 |
| α-helix | 140-147 | 8 | |
| β-strand | 154-157 | 4 | 3 |
| α-helix | 159-168 | 10 | |
| β-strand | 178-181 | 4 | 3 |
| α-helix | 184-187 | 4 | |
| α-helix | 188-192 | 5 | |
| α-helix | 193-200 | 8 | |
| β-strand | 208-212 | 5 | 3 |
| α-helix | 218-225 | 8 | |
| β-strand | 232-234 | 3 | 3 |
| β-strand | 247-252 | 6 | 4 |
| α-helix | 257-269 | 13 | |
| β-strand | 276-278 | 3 | 4 |
| α-helix | 282-293 | 12 | |
| β-strand | 300-301 | 2 | 4 |
| α-helix | 307-317 | 11 | |
| β-strand | 326-328 | 3 | 4 |
| α-helix | 332-335 | 4 | |
| α-helix | 338-340 | 3 | |
| β-strand | 343-346 | 4 | 4 |
| α-helix | 354-359 | 6 | |
| β-strand | 371-376 | 6 | 4 |
| α-helix | 380-390 | 11 | |
| β-strand | 396-397 | 2 | 4 |
| α-helix | 398 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic initiation factor 4A-I | A, D | protein | 414 | Homo sapiens | P60842 (AlphaFold model) |
| Programmed cell death protein 4 | C | protein | 358 | Mus musculus | Q61823 (AlphaFold model) |
>3EIQ_1 Eukaryotic initiation factor 4A-I (chains A, D) GPLGSPEFMSASQDSRSRDNGPDGMEPEGVIESNWNEIVDSFDDMNLSESLLRGIYAYGF EKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTREL AQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLS PKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPI RILVKKEELTLEGIRQFYINVEREEWKLDTLCDLYETLTITQAVIFINTRRKVDWLTEKM HARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTN RENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI
>3EIQ_2 Programmed cell death protein 4 (chains C) GPLGSPEFGKGVWGTPGQVYDVEEVDVKDPNYDDDQENCVYETVVLPLDETAFEKTLTPI IQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLALEGKASHREMTSKLLSDLCGTVM STNDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILCNTYIDSYKGTVDCVQA RAALDKATVLLSMSKGGKRKDSVWGSGGGQQPVNHLVKEIDMLLKEYLLSGDISEAEHCL KELEVPHFHHELVYEAIVMVLESTGESAFKMILDLLKSLWKSSTITIDQMKRGYERIYNE IPDINLDVPHSYSVLERFVEECFQAGIISKQLRDLCPSRGRKRFVSEGDGGRLKPESY
Structural basis for translational inhibition by the tumour suppressor Pdcd4. Loh, P.G., Yang, H.S., Walsh, M.A. et al. EMBO J (2009) 28:274-285. DOI 10.1038/emboj.2008.278 · PubMed
Other PDB entries of the same protein (UniProt P60842 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3EIQ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.