Structure of the PCI domain of translation initiation factor eIF3a. Determined by X-ray diffraction at 3.3 Å resolution. Released 10 Sept 2014.
Explore 4U1D in 3D Show helices and sheets RCSB PDB PDBe
4U1D contains 91 α-helices and 9 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 | 8-20 | 13 | |
| α-helix | 24-35 | 12 | |
| α-helix | 38-41 | 4 | |
| α-helix | 45-47 | 3 | |
| α-helix | 49-61 | 13 | |
| α-helix | 65-79 | 15 | |
| α-helix | 83-119 | 37 | |
| α-helix | 152-169 | 18 | |
| α-helix | 173-175 | 3 | |
| α-helix | 176-192 | 17 | |
| α-helix | 196-216 | 21 | |
| α-helix | 217-219 | 3 | |
| α-helix | 230-249 | 20 | |
| α-helix | 253-269 | 17 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-293 | 18 | |
| α-helix | 296-310 | 15 | |
| α-helix | 318-333 | 16 | |
| α-helix | 336-337 | 2 | |
| α-helix | 350-354 | 5 | |
| α-helix | 360-362 | 3 | |
| α-helix | 363-371 | 9 | |
| α-helix | 374-377 | 4 | |
| α-helix | 382-388 | 7 | |
| α-helix | 389-393 | 5 | |
| α-helix | 397-411 | 15 | |
| α-helix | 416-420 | 5 | |
| α-helix | 421-439 | 19 | |
| β-strand | 442-444 | 3 | 3 |
| α-helix | 445-451 | 7 | |
| α-helix | 454-455 | 2 | |
| α-helix | 462-474 | 13 | |
| β-strand | 480-483 | 4 | 3 |
| β-strand | 488-491 | 4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-20 | 13 | |
| α-helix | 24-35 | 12 | |
| α-helix | 38-41 | 4 | |
| α-helix | 45-47 | 3 | |
| α-helix | 49-61 | 13 | |
| α-helix | 65-79 | 15 | |
| α-helix | 83-110 | 28 | |
| α-helix | 152-169 | 18 | |
| α-helix | 173-175 | 3 | |
| α-helix | 176-192 | 17 | |
| α-helix | 196-217 | 22 | |
| α-helix | 230-249 | 20 | |
| α-helix | 253-269 | 17 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-293 | 18 | |
| α-helix | 296-310 | 15 | |
| α-helix | 318-333 | 16 | |
| α-helix | 336-337 | 2 | |
| α-helix | 350-354 | 5 | |
| α-helix | 360-362 | 3 | |
| α-helix | 363-372 | 10 | |
| α-helix | 374-377 | 4 | |
| α-helix | 382-388 | 7 | |
| α-helix | 389-393 | 5 | |
| α-helix | 397-411 | 15 | |
| α-helix | 416-420 | 5 | |
| α-helix | 421-439 | 19 | |
| β-strand | 442-444 | 3 | 2 |
| α-helix | 445-451 | 7 | |
| α-helix | 454-455 | 2 | |
| α-helix | 462-474 | 13 | |
| β-strand | 481-483 | 3 | 2 |
| β-strand | 488-490 | 3 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-20 | 13 | |
| α-helix | 24-35 | 12 | |
| α-helix | 38-41 | 4 | |
| α-helix | 45-47 | 3 | |
| α-helix | 49-61 | 13 | |
| α-helix | 65-79 | 15 | |
| α-helix | 83-106 | 24 | |
| α-helix | 152-169 | 18 | |
| α-helix | 176-192 | 17 | |
| α-helix | 196-216 | 21 | |
| α-helix | 217-219 | 3 | |
| α-helix | 230-249 | 20 | |
| α-helix | 253-269 | 17 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-293 | 18 | |
| α-helix | 296-310 | 15 | |
| α-helix | 318-333 | 16 | |
| α-helix | 336-337 | 2 | |
| α-helix | 351-354 | 4 | |
| α-helix | 360-362 | 3 | |
| α-helix | 363-371 | 9 | |
| α-helix | 374-377 | 4 | |
| α-helix | 382-388 | 7 | |
| α-helix | 389-393 | 5 | |
| α-helix | 397-411 | 15 | |
| α-helix | 416-420 | 5 | |
| α-helix | 421-439 | 19 | |
| β-strand | 442-444 | 3 | 1 |
| α-helix | 445-451 | 7 | |
| α-helix | 454-455 | 2 | |
| α-helix | 462-474 | 13 | |
| β-strand | 481-483 | 3 | 1 |
| β-strand | 488-490 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic translation initiation factor 3 subunit A | A, B, C | protein | 497 | Saccharomyces cerevisiae | P38249 (AlphaFold model) |
>4U1D_1 Eukaryotic translation initiation factor 3 subunit A (chains A, B, C) SNAMAPPPFRPENAIKRADELISVGEKQAALQSLHDFITARRIRWATPSTVEPVVFKFLE IGVELKKGKLLKDGLHQYKKLIQGSTEGLVSVGAVARKFIDLVESKIASEQTRADELQKQ EIDDDLEGGVTPENLLISVYESDQSVAGFNDEAITSWLRFTWESYRAVLDLLRNNALLEI TYSGVVKKTMHFCLKYQRKNEFKRLAEMLRQHLDAANYQQSKSGNNLVDLSDADTLQRYL DQRFQQVDVSVKLELWHEAYRSIEDVFHLMKISKRAPKPSTLANYYENLVKVFFVSGDPL LHTTAWKKFYKLYSTNPRATEEEFKTYSSTIFLSAISTQLDEIPSIGYDPHLRMYRLLNL DAKPTRKEMLQSIIEDESIYGKVDEELKELYDIIEVNFDVDTVKQQLENLLVKLSSKTYF SQYIAPLRDVIMRRVFVAASQKFTTVSQSELYKLATLPAPLDLSAWDIEKSLLQAAVEDY VSITIDHESAKVTFAKD
Molecular Architecture of the 40SeIF1eIF3 Translation Initiation Complex. Erzberger, J.P., Stengel, F., Pellarin, R. et al. Cell (2014) 158:1123-1135. DOI 10.1016/j.cell.2014.07.044 · PubMed
Other PDB entries of the same protein (UniProt P38249 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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