Crystal structure of the CBC-importin alpha complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 11 Aug 2009.
Explore 3FEY in 3D Show helices and sheets RCSB PDB PDBe
3FEY contains 82 α-helices and 15 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 | 24-37 | 14 | |
| α-helix | 46-78 | 33 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-96 | 14 | |
| α-helix | 98-117 | 20 | |
| α-helix | 121-133 | 13 | |
| β-strand | 140 | 1 | 1 |
| α-helix | 142-153 | 12 | |
| α-helix | 154-157 | 4 | |
| α-helix | 163-187 | 25 | |
| α-helix | 189-205 | 17 | |
| α-helix | 211-214 | 4 | |
| β-strand | 217 | 1 | 2 |
| β-strand | 227 | 1 | 3 |
| α-helix | 228-241 | 14 | |
| α-helix | 252-256 | 5 | |
| α-helix | 257-262 | 6 | |
| β-strand | 266 | 1 | 1 |
| α-helix | 267-270 | 4 | |
| α-helix | 273-276 | 4 | |
| α-helix | 283-285 | 3 | |
| β-strand | 287 | 1 | 3 |
| α-helix | 294-296 | 3 | |
| α-helix | 302-305 | 4 | |
| α-helix | 309-325 | 17 | |
| α-helix | 329-337 | 9 | |
| α-helix | 347-359 | 13 | |
| α-helix | 369-382 | 14 | |
| α-helix | 387-400 | 14 | |
| α-helix | 402-404 | 3 | |
| β-strand | 405 | 1 | 2 |
| α-helix | 407-422 | 16 | |
| α-helix | 430-438 | 9 | |
| α-helix | 444-458 | 15 | |
| α-helix | 462-468 | 7 | |
| α-helix | 471-476 | 6 | |
| α-helix | 478-480 | 3 | |
| α-helix | 498-509 | 12 | |
| α-helix | 514-521 | 8 | |
| α-helix | 541-554 | 14 | |
| α-helix | 559-568 | 10 | |
| α-helix | 570-576 | 7 | |
| α-helix | 580-594 | 15 | |
| α-helix | 598-610 | 13 | |
| α-helix | 616-623 | 8 | |
| α-helix | 626-631 | 6 | |
| α-helix | 635-665 | 31 | |
| α-helix | 684-731 | 48 | |
| α-helix | 738-758 | 21 | |
| α-helix | 759-761 | 3 | |
| α-helix | 762-764 | 3 | |
| α-helix | 765-769 | 5 | |
| α-helix | 776-786 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-38 | 8 | |
| β-strand | 41-45 | 5 | 4 |
| α-helix | 53-60 | 8 | |
| α-helix | 61-63 | 3 | |
| β-strand | 66-73 | 8 | 4 |
| β-strand | 80-88 | 9 | 4 |
| α-helix | 91-100 | 10 | |
| β-strand | 105-106 | 2 | 5 |
| β-strand | 109-110 | 2 | 5 |
| β-strand | 112-116 | 5 | 4 |
| β-strand | 125 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 71 | 1 | 6 |
| β-strand | 74 | 1 | 6 |
| α-helix | 78-85 | 8 | |
| α-helix | 90-104 | 15 | |
| α-helix | 112-117 | 6 | |
| α-helix | 120-129 | 10 | |
| α-helix | 134-147 | 14 | |
| α-helix | 152-160 | 9 | |
| α-helix | 163-170 | 8 | |
| α-helix | 176-190 | 15 | |
| α-helix | 194-202 | 9 | |
| α-helix | 206-211 | 6 | |
| α-helix | 223-236 | 14 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-259 | 14 | |
| α-helix | 265-279 | 15 | |
| α-helix | 283-291 | 9 | |
| α-helix | 295-301 | 7 | |
| α-helix | 307-320 | 14 | |
| α-helix | 325-333 | 9 | |
| α-helix | 336-344 | 9 | |
| α-helix | 349-362 | 14 | |
| α-helix | 367-375 | 9 | |
| α-helix | 379-388 | 10 | |
| α-helix | 391-407 | 17 | |
| α-helix | 410-418 | 9 | |
| α-helix | 422-427 | 6 | |
| α-helix | 428-430 | 3 | |
| α-helix | 434-454 | 21 | |
| α-helix | 457-466 | 10 | |
| α-helix | 469-475 | 7 | |
| α-helix | 476-478 | 3 | |
| α-helix | 482-495 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear cap-binding protein subunit 1 | A | protein | 790 | Homo sapiens | Q09161 (AlphaFold model) |
| Nuclear cap-binding protein subunit 2 | B | protein | 156 | Homo sapiens | P52298 (AlphaFold model) |
| Importin subunit alpha-2 | C | protein | 467 | Homo sapiens | P52292 (AlphaFold model) |
>3FEY_1 Nuclear cap-binding protein subunit 1 (chains A) MSRRRHSDENDGGQPHKRRKTSDANETEDHLESLICKVGEKSACSLESNLEGLAGVLEAD LPNYKSKILRLLCTVARLLPEKLTIYTTLVGLLNARNYNFGGEFVEAMIRQLKESLKANN YNEAVYLVRFLSDLVNCHVIAAPSMVAMFENFVSVTQEEDVPQVRRDWYVYAFLSSLPWV GKELYEKKDAEMDRIFANTESYLKRRQKTHVPMLQVWTADKPHPQEEYLDCLWAQIQKLK KDRWQERHILRPYLAFDSILCEALQHNLPPFTPPPHTEDSVYPMPRVIFRMFDYTDDPEG PVMPGSHSVERFVIEENLHCIIKSHWKERKTCAAQLVSYPGKNKIPLNYHIVEVIFAELF QLPAPPHIDVMYTTLLIELCKLQPGSLPQVLAQATEMLYMRLDTMNTTCVDRFINWFSHH LSNFQFRWSWEDWSDCLSQDPESPKPKFVREVLEKCMRLSYHQRILDIVPPTFSALCPAN PTCIYKYGDESSNSLPGHSVALCLAVAFKSKATNDEIFSILKDVPNPNQDDDDDEGFSFN PLKIEVFVQTLLHLAAKSFSHSFSALAKFHEVFKTLAESDEGKLHVLRVMFEVWRNHPQM IAVLVDKMIRTQIVDCAAVANWIFSSELSRDFTRLFVWEILHSTIRKMNKHVLKIQKELE EAKEKLARQHKRRSDDDDRSSDRKDGVLEEQIERLQEKVESAQSEQKNLFLVIFQRFIMI LTEHLVRCETDGTSVLTPWYKNCIERLQQIFLQHHQIIQQYMVTLENLLFTAELDPHILA VFQQFCALQA
>3FEY_2 Nuclear cap-binding protein subunit 2 (chains B) MSGGLLKALRSDSYVELSQYRDQHFRGDNEEQEKLLKKSCTLYVGNLSFYTTEEQIYELF SKSGDIKKIIMGLDKMKKTACGFCFVEYYSRADAENAMRYINGTRLDDRIIRTDWDAGFK EGRQYGRGRSGGQVRDEYRQDYDAGRGGYGKLAQNQ
>3FEY_3 Importin subunit alpha-2 (chains C) MNQGTVNWSVDDIVKGINSSNVENQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFL GRTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGN IAGDGSVFRDLVIKYGAVDPLLALLAVPDMSSLACGYLRNLTWTLSNLCRNKNPAPPIDA VEQILPTLVRLLHHDDPEVLADTCWAISYLTDGPNERIGMVVKTGVVPQLVKLLGASELP IVTPALRAIGNIVTGTDEQTQVVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQD QIQQVVNHGLVPFLVSVLSKADFKTQKEAVWAVTNYTSGGTVEQIVYLVHCGIIEPLMNL LTAKDTKIILVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQNHENESVYKAS LSLIEKYFSVEEEEDQNVVPETTSEGYTFQVQDGAPGTFNFHHHHHH
The molecular basis for the regulation of the cap-binding complex by the importins. Dias, S.M., Wilson, K.F., Rojas, K.S. et al. Nat Struct Mol Biol (2009) 16:930-937. DOI 10.1038/nsmb.1649 · PubMed
Other PDB entries of the same protein (UniProt Q09161 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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