Cryo-EM structure of yeast Exportin Msn5 bound to RanGTP and Pho4 (not modeled) (State 2-1). Determined by electron microscopy at 3.2 Å resolution. Released 19 Mar 2025.
Explore 9DXM in 3D Show helices and sheets RCSB PDB PDBe
9DXM contains 78 α-helices and 11 β-strands across 2 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 | 6-17 | 12 | |
| α-helix | 23-38 | 16 | |
| α-helix | 42-52 | 11 | |
| α-helix | 57-73 | 17 | |
| α-helix | 80-95 | 16 | |
| α-helix | 103-120 | 18 | |
| α-helix | 123-126 | 4 | |
| α-helix | 132-137 | 6 | |
| α-helix | 142-152 | 11 | |
| α-helix | 154-168 | 15 | |
| α-helix | 169-173 | 5 | |
| α-helix | 177-180 | 4 | |
| α-helix | 183-194 | 12 | |
| α-helix | 197-203 | 7 | |
| α-helix | 208-211 | 4 | |
| α-helix | 221-234 | 14 | |
| α-helix | 237-247 | 11 | |
| α-helix | 256-262 | 7 | |
| α-helix | 264-272 | 9 | |
| α-helix | 277-292 | 16 | |
| α-helix | 298-310 | 13 | |
| α-helix | 312-322 | 11 | |
| α-helix | 335-346 | 12 | |
| α-helix | 348-354 | 7 | |
| α-helix | 361-373 | 13 | |
| α-helix | 378-392 | 15 | |
| α-helix | 398-404 | 7 | |
| α-helix | 406-415 | 10 | |
| α-helix | 420-422 | 3 | |
| α-helix | 429-435 | 7 | |
| α-helix | 439-463 | 25 | |
| α-helix | 465-479 | 15 | |
| α-helix | 483-489 | 7 | |
| α-helix | 499-524 | 26 | |
| α-helix | 531-550 | 20 | |
| α-helix | 557-570 | 14 | |
| α-helix | 576-590 | 15 | |
| α-helix | 604-626 | 23 | |
| α-helix | 628-632 | 5 | |
| α-helix | 635-645 | 11 | |
| α-helix | 646-648 | 3 | |
| α-helix | 651-667 | 17 | |
| α-helix | 673-685 | 13 | |
| α-helix | 686-689 | 4 | |
| α-helix | 691-696 | 6 | |
| α-helix | 700-707 | 8 | |
| α-helix | 709-718 | 10 | |
| α-helix | 727-729 | 3 | |
| β-strand | 731 | 1 | 1 |
| α-helix | 732 | 1 | |
| α-helix | 734-750 | 17 | |
| α-helix | 753-763 | 11 | |
| α-helix | 770-784 | 15 | |
| α-helix | 788-801 | 14 | |
| α-helix | 807-809 | 3 | |
| α-helix | 812-814 | 3 | |
| α-helix | 815-821 | 7 | |
| β-strand | 849 | 1 | 1 |
| α-helix | 850-876 | 27 | |
| α-helix | 880-883 | 4 | |
| α-helix | 888-896 | 9 | |
| α-helix | 912-918 | 7 | |
| α-helix | 919-923 | 5 | |
| α-helix | 924-928 | 5 | |
| α-helix | 935-959 | 25 | |
| α-helix | 979-1002 | 24 | |
| α-helix | 1018-1029 | 12 | |
| α-helix | 1031-1046 | 16 | |
| α-helix | 1050-1067 | 18 | |
| α-helix | 1073-1077 | 5 | |
| α-helix | 1078-1082 | 5 | |
| α-helix | 1083-1085 | 3 | |
| α-helix | 1102-1114 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-19 | 8 | 2 |
| α-helix | 25-33 | 9 | |
| β-strand | 47-56 | 10 | 2 |
| β-strand | 59-68 | 10 | 2 |
| α-helix | 80-82 | 3 | |
| β-strand | 87-93 | 7 | 2 |
| α-helix | 97-101 | 5 | |
| α-helix | 103-111 | 9 | |
| β-strand | 119-124 | 6 | 2 |
| α-helix | 140-144 | 5 | |
| β-strand | 147-150 | 4 | 2 |
| β-strand | 152 | 1 | 3 |
| β-strand | 155 | 1 | 3 |
| α-helix | 156-158 | 3 | |
| α-helix | 161-171 | 11 | |
| β-strand | 178-179 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein MSN5 | A | protein | 1230 | Saccharomyces cerevisiae | P52918 (AlphaFold model) |
| GTP-binding nuclear protein GSP1/CNR1 | B | protein | 186 | Saccharomyces cerevisiae | P32835 (AlphaFold model) |
>9DXM_1 Protein MSN5 (chains A) MDSTGASQIVSALDVIYSPKSNNSQRQEAQKFLDEVKLCSESPFWGYEIALQNPTNSILK YFGLGLLDHAVKKNWNDYDEGKRVALRKWVMELNFGVQDYDTRYIKEKLATLWVEVAKRT WGEALKQTNPTEEQLLTSWVDMDNNLFELWNINQSSRELALIIFRILFEDVFLLDDLIVL KRMTVIQPLCVMIVCPIEVFAIKYKFSDKWTKFKANEEGWFSVWIPELNNALQQNNSEYI IRLLETLKTCLNWPLTEVIVRNDVLSSLLTCLSSNIPRAQSMALDSIHILLTRPYSNESH YQMTIDRVFDNMDLLDSVYESLLFDPTDDIDETKYPIIKKFVDMISCLYVCVPKIKETNG QIQKYFKLVLKTTYNPSLIVSGLTLDLWCTCLRNDEYLPKLEKYVIPDLLQFAADALVYY EQIDGHISKKFAEIDFQSKSEFQTFCSTYRKRIRDIIRLISCVELDLTYDWLNNRLNNYF SSPFGQQVLSSTFLDHKLEPYLGALSQYMIVECFINGCIRWKIWYPTGDDYDEKLDSILQ KLEILSNQLIALNLREPLLLKKQIQNFALFLTMLKDNVLFTLLEKIITSATMDYPEINLE ERGAESDAVRDLRYACGIELNRMALLMPESLKKIYPDLESVIARIMPNLSYHEKISFKSF LLIIVLKSSLDMKEERFAAIVDPELLAWSDKTTVVGLSDLHWFMERLGIVQIAEYFQRRD IDENSDLLSIPIDDEGKELKSELTKRWQSLFPVRATRMFIHYSMQSIKTDEEFKMLQDLW RPRIVPILPYITRLLYQLQSYHDPDNWKGLPTVVQSFVKYSTIERFWEAGASNKSKDEFI DEHMKAMQTLRDFADSVGHIIRYTREYTLLVLSAISSLGSVFYLLDESPDLLLNSIAIFK PGSNEISPGVSTHGWKHIMNIAIRPILKGCPKDCLGKFMPAFLPKLFEILDLLLCQKWSS HMNDMDMNPVPTDDDQMTEEILEENLLRQLTTVVVRIVIDCVGQGNANPNSAKSRLNNHQ MEMRKIIFNDLNTLAPFLKLLNHLISFKDTKCSFNSILVMKCCLTSVLNQNNTVDEYFTF EVMKNLLLNVLCNSAFKDSFHEALYAFTVIFLTLCKEYPSARAFLFEISNGYNIDELYRN LRSVDEYKTQRALMIDFIDWVKSTSGKEDGNVDHAGDERKRQEKREAILKKANERLIKKN KENGDMLDDPNIEDGAVGNLFDDNENLYFQ
>9DXM_2 GTP-binding nuclear protein GSP1/CNR1 (chains B) MASAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFG EIKFDVWDTAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPI VLCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFV ENLYFQ
Phosphate-dependent nuclear export via a non-classical NES class recognized by exportin Msn5. Fung, H.Y.J., Mittal, S.R., Niesman, A.B. et al. Nat Commun (2025) 16:2580-2580. DOI 10.1038/s41467-025-57752-3 · PubMed
Other PDB entries of the same protein (UniProt P52918 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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