Crystal structure of yeast CRM1 (Xpo1p) in complex with yeast RanBP1 (Yrb1p) and yeast RanGTP (Gsp1pGTP). Determined by X-ray diffraction at 2.0 Å resolution. Released 2 Jun 2010.
Explore 3M1I in 3D Show helices and sheets RCSB PDB PDBe
3M1I contains 82 α-helices and 16 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 | 47-57 | 11 | 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 |
| α-helix | 161-171 | 11 | |
| β-strand | 178 | 1 | 1 |
| α-helix | 180-182 | 3 | |
| α-helix | 184-187 | 4 | |
| α-helix | 200-207 | 8 | |
| α-helix | 210-211 | 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 | 1 | 2 |
| β-strand | 155-163 | 9 | 2 |
| β-strand | 170-177 | 8 | 2 |
| α-helix | 181-199 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-5 | 6 | |
| α-helix | 10-11 | 2 | |
| α-helix | 13-25 | 13 | |
| α-helix | 28-43 | 16 | |
| α-helix | 47-50 | 4 | |
| α-helix | 51-57 | 7 | |
| 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 | 137-145 | 9 | |
| α-helix | 149-163 | 15 | |
| α-helix | 164-168 | 5 | |
| α-helix | 176-203 | 28 | |
| α-helix | 207-220 | 14 | |
| α-helix | 227-230 | 4 | |
| α-helix | 234-239 | 6 | |
| α-helix | 241-244 | 4 | |
| α-helix | 246-261 | 16 | |
| α-helix | 262-264 | 3 | |
| 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 | 443-445 | 3 | 3 |
| β-strand | 451-453 | 3 | 3 |
| α-helix | 459-478 | 20 | |
| α-helix | 480-495 | 16 | |
| α-helix | 502-514 | 13 | |
| α-helix | 521-538 | 18 | |
| α-helix | 545-561 | 17 | |
| α-helix | 563-568 | 6 | |
| α-helix | 570-583 | 14 | |
| α-helix | 589-606 | 18 | |
| 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 | 783-788 | 6 | |
| α-helix | 789-801 | 13 | |
| α-helix | 804-806 | 3 | |
| α-helix | 810-822 | 13 | |
| 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 | 978-980 | 3 | |
| α-helix | 987-1002 | 16 | |
| α-helix | 1008-1020 | 13 | |
| α-helix | 1025-1039 | 15 | |
| α-helix | 1046-1054 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTP-binding nuclear protein GSP1/CNR1 | A | protein | 219 | Saccharomyces cerevisiae | P32835 (AlphaFold model) |
| Ran-specific GTPase-activating protein 1 | B | protein | 191 | Saccharomyces cerevisiae | P41920 (AlphaFold model) |
| Exportin-1 | C | protein | 1049 | Saccharomyces cerevisiae | P30822 (AlphaFold model) |
>3M1I_1 GTP-binding nuclear protein GSP1/CNR1 (chains A) MSAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGE IKFDVWDTAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIV LCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVA SPALAPPEVQVDEQLMQQYQQEMEQATALPLPDEDDADL
>3M1I_2 Ran-specific GTPase-activating protein 1 (chains B) DKKEEAAPKPPSSAVFSMFGGKKAEKPETKKDEEDTKEETKKEGDDAPESPDIHFEPVVH LEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKKTNKVRILMRRDK TLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRFGSKENADKFKEE FEKAQEINKKA
>3M1I_3 Exportin-1 (chains C) GAMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFS TNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKS DLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQAK ALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELL STKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLK ATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEEREL FKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREF VKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSI SGTMSEDTEKRFVVTVIKDLLDLTVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRT VILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTAD LQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSET VKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPK VRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCM TTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFL ELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIF VSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYL ANMLSNAFPHLTSEQIASFLSALTKQYKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDK ENALMEQNRLEREKAAKIGGLLKPSELDD
An allosteric mechanism to displace nuclear export cargo from CRM1 and RanGTP by RanBP1. Koyama, M., Matsuura, Y. EMBO J (2010) 29:2002-2013. DOI 10.1038/emboj.2010.89 · 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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