MVM NES mutant Nm12 in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 2.35 Å resolution. Released 19 Jun 2019.
Explore 6A3C in 3D Show helices and sheets RCSB PDB PDBe
6A3C contains 85 α-helices and 14 β-strands across 4 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 | 10-17 | 8 | 1 |
| α-helix | 23-32 | 10 | |
| β-strand | 45-55 | 11 | 1 |
| β-strand | 57-66 | 10 | 1 |
| α-helix | 70-72 | 3 | |
| α-helix | 76-80 | 5 | |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 133-135 | 3 | |
| α-helix | 139-142 | 4 | |
| β-strand | 145-148 | 4 | 1 |
| α-helix | 159-169 | 11 | |
| β-strand | 176 | 1 | 1 |
| α-helix | 178-180 | 3 | |
| α-helix | 182-185 | 4 | |
| α-helix | 187-190 | 4 | |
| α-helix | 194-205 | 12 | |
| α-helix | 208-209 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 83-97 | 15 | 2 |
| β-strand | 102-116 | 15 | 2 |
| β-strand | 122-127 | 6 | 2 |
| β-strand | 134-139 | 6 | 2 |
| β-strand | 147-149 | 3 | 2 |
| β-strand | 152-163 | 12 | 2 |
| β-strand | 170-178 | 9 | 2 |
| α-helix | 181-198 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-5 | 6 | |
| α-helix | 10-11 | 2 | |
| α-helix | 13-24 | 12 | |
| α-helix | 28-42 | 15 | |
| α-helix | 47-50 | 4 | |
| α-helix | 52-57 | 6 | |
| α-helix | 61-77 | 17 | |
| α-helix | 79-81 | 3 | |
| α-helix | 84-103 | 20 | |
| α-helix | 105-110 | 6 | |
| α-helix | 112-129 | 18 | |
| α-helix | 137-147 | 11 | |
| α-helix | 149-163 | 15 | |
| α-helix | 164-168 | 5 | |
| α-helix | 170-173 | 4 | |
| α-helix | 176-188 | 13 | |
| α-helix | 190-203 | 14 | |
| 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 | 246-260 | 15 | |
| 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 | 418-420 | 3 | |
| α-helix | 421-433 | 13 | |
| α-helix | 462-478 | 17 | |
| α-helix | 480-495 | 16 | |
| α-helix | 502-514 | 13 | |
| 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 | 638-654 | 17 | |
| 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 | 754-775 | 22 | |
| α-helix | 780-782 | 3 | |
| α-helix | 783-788 | 6 | |
| α-helix | 789-801 | 13 | |
| 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 | 872-875 | 4 | |
| α-helix | 879-893 | 15 | |
| α-helix | 898-918 | 21 | |
| α-helix | 922-944 | 23 | |
| α-helix | 949-951 | 3 | |
| α-helix | 952-967 | 16 | |
| α-helix | 987-1002 | 16 | |
| α-helix | 1008-1020 | 13 | |
| α-helix | 1025-1038 | 14 | |
| α-helix | 1046-1050 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 78-87 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTP-binding nuclear protein Ran | A | protein | 235 | Homo sapiens | P62826 (AlphaFold model) |
| Ran-specific GTPase-activating protein 1 | B | protein | 143 | Saccharomyces cerevisiae | P41920 (AlphaFold model) |
| Exportin-1 | C | protein | 1003 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P30822 (AlphaFold model) |
| MVM NES mutant Nm12 | D | protein | 21 | Minute virus of mice | P0DJZ2 (AlphaFold model) |
>6A3C_1 GTP-binding nuclear protein Ran (chains A) GSSHHHHHHSSGLVPRGSHMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVA TLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNV PNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPF LWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQAEHDLEVAQTTALPDEDDDL
>6A3C_2 Ran-specific GTPase-activating protein 1 (chains B) GGSDIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKK TNKVRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRF GSKENADKFKEEFEKAQEINKKA
>6A3C_3 Exportin-1 (chains C) GGSMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQF STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEIQLYKSEREVLVYL THLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDL LGLCEQKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMA CDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQVHTFYKACGIIISEE RSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGA DFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVRGLRTIKKEILKLVETYIS KARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQ SVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPAAFKLFVDAICWAFKH NNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQ ALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFL SALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENA
>6A3C_4 MVM NES mutant Nm12 (chains D) GGSTVDEMTKKFGTLTIHDDD
Water and common crystallization additives (CL, GOL, EDO, NA) are not listed.
Cancer Therapy with Nanoparticle-Medicated Intracellular Expression of Peptide CRM1-Inhibitor. Sui, M., Xiong, M., Li, Y. et al. Int J Nanomedicine (2021) 16:2833-2847. DOI 10.2147/IJN.S266398 · PubMed
Other PDB entries of the same protein (UniProt P62826 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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