Cryo-EM structure of unliganded yeast Exportin Msn5. Determined by electron microscopy at 3.39 Å resolution. Released 19 Mar 2025.
Explore 9D43 in 3D Show helices and sheets RCSB PDB PDBe
9D43 contains 77 α-helices and 4 β-strands across 1 chain. 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 | 22-37 | 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 | 131-137 | 7 | |
| α-helix | 142-150 | 9 | |
| α-helix | 154-169 | 16 | |
| α-helix | 170-174 | 5 | |
| α-helix | 177-181 | 5 | |
| α-helix | 183-194 | 12 | |
| α-helix | 197-203 | 7 | |
| α-helix | 210-213 | 4 | |
| α-helix | 221-234 | 14 | |
| α-helix | 237-250 | 14 | |
| 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 | 335-347 | 13 | |
| α-helix | 348-354 | 7 | |
| α-helix | 361-373 | 13 | |
| α-helix | 378-383 | 6 | |
| α-helix | 385-393 | 9 | |
| α-helix | 398-401 | 4 | |
| α-helix | 406-416 | 11 | |
| α-helix | 428-435 | 8 | |
| α-helix | 439-463 | 25 | |
| α-helix | 465-481 | 17 | |
| α-helix | 486-489 | 4 | |
| α-helix | 499-524 | 26 | |
| α-helix | 530-551 | 22 | |
| α-helix | 557-574 | 18 | |
| α-helix | 575-577 | 3 | |
| α-helix | 579-591 | 13 | |
| α-helix | 604-626 | 23 | |
| α-helix | 630-632 | 3 | |
| α-helix | 635-644 | 10 | |
| α-helix | 650-667 | 18 | |
| α-helix | 673-685 | 13 | |
| α-helix | 686-689 | 4 | |
| α-helix | 691-696 | 6 | |
| α-helix | 700-707 | 8 | |
| α-helix | 709-719 | 11 | |
| β-strand | 731 | 1 | 1 |
| α-helix | 732-733 | 2 | |
| α-helix | 734-750 | 17 | |
| α-helix | 753-763 | 11 | |
| α-helix | 771-784 | 14 | |
| α-helix | 788-801 | 14 | |
| α-helix | 806-809 | 4 | |
| α-helix | 812-814 | 3 | |
| α-helix | 815-822 | 8 | |
| β-strand | 849 | 1 | 1 |
| α-helix | 850-878 | 29 | |
| α-helix | 880-883 | 4 | |
| α-helix | 887-896 | 10 | |
| β-strand | 899 | 1 | 2 |
| β-strand | 906 | 1 | 2 |
| α-helix | 912-918 | 7 | |
| α-helix | 919-923 | 5 | |
| α-helix | 924-928 | 5 | |
| α-helix | 935-959 | 25 | |
| α-helix | 969-972 | 4 | |
| α-helix | 979-1002 | 24 | |
| α-helix | 1019-1028 | 10 | |
| α-helix | 1031-1046 | 16 | |
| α-helix | 1051-1063 | 13 | |
| α-helix | 1064-1066 | 3 | |
| α-helix | 1072-1077 | 6 | |
| α-helix | 1078-1082 | 5 | |
| α-helix | 1083-1086 | 4 | |
| α-helix | 1087-1091 | 5 | |
| α-helix | 1100-1117 | 18 | |
| α-helix | 1119-1129 | 11 | |
| α-helix | 1134-1142 | 9 | |
| α-helix | 1147-1165 | 19 | |
| α-helix | 1176-1197 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein MSN5 | A | protein | 1230 | Saccharomyces cerevisiae | P52918 (AlphaFold model) |
>9D43_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
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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