Crystal structure of Xpo1p-PKI-Gsp1p-GTP complex. Determined by X-ray diffraction at 2.15 Å resolution. Released 12 Nov 2014.
Explore 3WYG in 3D Show helices and sheets RCSB PDB PDBe
3WYG contains 76 α-helices and 13 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 | 12-19 | 8 | 1 |
| α-helix | 25-34 | 10 | |
| β-strand | 47-56 | 10 | 1 |
| β-strand | 59-68 | 10 | 1 |
| α-helix | 72-74 | 3 | |
| α-helix | 78-82 | 5 | |
| β-strand | 87-93 | 7 | 1 |
| α-helix | 97-101 | 5 | |
| α-helix | 103-113 | 11 | |
| β-strand | 119-124 | 6 | 1 |
| α-helix | 135-137 | 3 | |
| α-helix | 140-144 | 5 | |
| β-strand | 147-150 | 4 | 1 |
| β-strand | 152 | 1 | 2 |
| β-strand | 157 | 1 | 2 |
| α-helix | 161-171 | 11 | |
| β-strand | 178 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-25 | 13 | |
| α-helix | 28-43 | 16 | |
| α-helix | 49-57 | 9 | |
| α-helix | 61-78 | 18 | |
| α-helix | 79-81 | 3 | |
| α-helix | 84-103 | 20 | |
| α-helix | 105-110 | 6 | |
| α-helix | 112-129 | 18 | |
| α-helix | 137-146 | 10 | |
| α-helix | 149-163 | 15 | |
| α-helix | 164-168 | 5 | |
| β-strand | 171 | 1 | 3 |
| β-strand | 174 | 1 | 3 |
| α-helix | 176-203 | 28 | |
| α-helix | 207-220 | 14 | |
| α-helix | 227-230 | 4 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-241 | 5 | |
| α-helix | 242-244 | 3 | |
| α-helix | 246-248 | 3 | |
| α-helix | 249-259 | 11 | |
| α-helix | 269-289 | 21 | |
| α-helix | 297-303 | 7 | |
| α-helix | 308-331 | 24 | |
| α-helix | 334-336 | 3 | |
| α-helix | 337-351 | 15 | |
| α-helix | 356-375 | 20 | |
| α-helix | 417-420 | 4 | |
| α-helix | 421-433 | 13 | |
| β-strand | 441-445 | 5 | 4 |
| β-strand | 451-455 | 5 | 4 |
| α-helix | 460-478 | 19 | |
| α-helix | 480-495 | 16 | |
| α-helix | 502-513 | 12 | |
| α-helix | 521-541 | 21 | |
| α-helix | 545-560 | 16 | |
| α-helix | 563-568 | 6 | |
| α-helix | 570-583 | 14 | |
| α-helix | 591-606 | 16 | |
| α-helix | 608-611 | 4 | |
| α-helix | 613-614 | 2 | |
| α-helix | 621-627 | 7 | |
| α-helix | 629-633 | 5 | |
| α-helix | 638-653 | 16 | |
| α-helix | 658-668 | 11 | |
| α-helix | 670-685 | 16 | |
| α-helix | 687-691 | 5 | |
| α-helix | 693-713 | 21 | |
| α-helix | 714-717 | 4 | |
| α-helix | 718-746 | 29 | |
| α-helix | 748-752 | 5 | |
| α-helix | 754-776 | 23 | |
| α-helix | 780-782 | 3 | |
| α-helix | 783-787 | 5 | |
| α-helix | 788-801 | 14 | |
| α-helix | 804-806 | 3 | |
| α-helix | 809-822 | 14 | |
| α-helix | 823-825 | 3 | |
| α-helix | 827-845 | 19 | |
| α-helix | 853-869 | 17 | |
| α-helix | 872-876 | 5 | |
| α-helix | 879-893 | 15 | |
| α-helix | 898-917 | 20 | |
| α-helix | 922-944 | 23 | |
| α-helix | 949-951 | 3 | |
| α-helix | 952-967 | 16 | |
| α-helix | 987-1002 | 16 | |
| α-helix | 1008-1021 | 14 | |
| α-helix | 1025-1038 | 14 | |
| α-helix | 1046-1050 | 5 | |
| α-helix | 1051-1054 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-43 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gsp1p | A | protein | 182 | Saccharomyces cerevisiae AWRI796 | P32835 (AlphaFold model) |
| Exportin-1 | C | protein | 1049 | Saccharomyces cerevisiae S288c | P30822 (AlphaFold model) |
| cAMP-dependent protein kinase inhibitor alpha | D | protein | 76 | Homo sapiens | P61925 (AlphaFold model) |
>3WYG_1 Gsp1p (chains A) MSAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGE IKFDVWDTAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIV LCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVA SP
>3WYG_2 Exportin-1 (chains C) GAMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFS TNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKS DLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQAK ALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELL STKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLK ATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEEREL FKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREF VKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSI SGTMSEDTEKRFVVTVIKDLLDLTVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRT VILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTAD LQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSET VKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPK VRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCM TTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFL ELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIF VSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYL ANMLSNAFPHLTSEQIASFLSALTKQYKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDK ENALMEQNRLEREKAAKIGGLLKPSELDD
>3WYG_3 cAMP-dependent protein kinase inhibitor alpha (chains D) MTDVETTYADFIASGRTGRRNAIHDILVSSASGNLNELALKLAGLDINKTEGEEDAQRSS TEQSGEAQGEAAKSES
Structural insights into how yrb2p accelerates the assembly of the xpo1p nuclear export complex. Koyama, M., Shirai, N., Matsuura, Y. Cell Rep (2014) 9:983-995. DOI 10.1016/j.celrep.2014.09.052 · PubMed
Other PDB entries of the same protein (UniProt P32835 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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