Yeast CRM1e (apo) in complex with Ran-RanBP1. Determined by X-ray diffraction at 2.06 Å resolution. Released 29 Sept 2021.
Explore 7DBG in 3D Show helices and sheets RCSB PDB PDBe
7DBG contains 84 α-helices and 14 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 | 9-16 | 8 | 1 |
| α-helix | 23-32 | 10 | |
| β-strand | 45-54 | 10 | 1 |
| β-strand | 57-66 | 10 | 1 |
| α-helix | 70-72 | 3 | |
| α-helix | 76-79 | 4 | |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-109 | 9 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 133-135 | 3 | |
| α-helix | 138-142 | 5 | |
| β-strand | 145-148 | 4 | 1 |
| α-helix | 159-169 | 11 | |
| β-strand | 176 | 1 | 1 |
| α-helix | 178-180 | 3 | |
| α-helix | 182-186 | 5 | |
| α-helix | 191-193 | 3 | |
| α-helix | 194-197 | 4 | |
| α-helix | 201-205 | 5 | |
| 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 | 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 | 1-5 | 5 | |
| 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 | 170-173 | 4 | |
| 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 | 246-260 | 15 | |
| α-helix | 269-289 | 21 | |
| α-helix | 297-303 | 7 | |
| α-helix | 308-326 | 19 | |
| α-helix | 327-330 | 4 | |
| α-helix | 334-336 | 3 | |
| α-helix | 337-350 | 14 | |
| α-helix | 356-375 | 20 | |
| α-helix | 417-420 | 4 | |
| α-helix | 421-433 | 13 | |
| α-helix | 435-437 | 3 | |
| α-helix | 462-478 | 17 | |
| α-helix | 480-495 | 16 | |
| α-helix | 502-514 | 13 | |
| α-helix | 521-541 | 21 | |
| α-helix | 545-561 | 17 | |
| α-helix | 563-568 | 6 | |
| α-helix | 570-583 | 14 | |
| α-helix | 591-606 | 16 | |
| α-helix | 608-611 | 4 | |
| α-helix | 621-627 | 7 | |
| α-helix | 629-633 | 5 | |
| α-helix | 638-652 | 15 | |
| 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 | 788-800 | 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 | 898-917 | 20 | |
| α-helix | 922-944 | 23 | |
| α-helix | 949-951 | 3 | |
| α-helix | 952-967 | 16 | |
| α-helix | 977 | 1 | |
| α-helix | 987-1002 | 16 | |
| α-helix | 1008-1020 | 13 | |
| α-helix | 1025-1038 | 14 | |
| α-helix | 1046-1050 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTP-binding nuclear protein Ran | A | protein | 216 | Homo sapiens | P62826 (AlphaFold model) |
| YRB1 isoform 1 | B | protein | 140 | Saccharomyces cerevisiae | P41920 (AlphaFold model) |
| CRM1 isoform 1 | C | protein | 1003 | Saccharomyces cerevisiae | P30822 (AlphaFold model) |
>7DBG_1 GTP-binding nuclear protein Ran (chains A) MAAQGEPEVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK FNVWDTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP AAAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
>7DBG_2 YRB1 isoform 1 (chains B) DIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKKTNK VRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRFGSK ENADKFKEEFEKAQEINKKA
>7DBG_3 CRM1 isoform 1 (chains C) GGSMEGILDFSNDLDIALLDQVVSTFYQGEGVQQKQAQEILTKFQDNPDAWEKVDQILQF STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEIQLYKSEREVLVYL THLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDL LGLCEQKRGKDNKAVVARDIMYVVGEYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMA CDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQVHTFYKACGIIISEE RSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGA DFYPQLGHIYYNMLQLYRAVSSMISTQVAAEGLIATKTPKVRGLRTIKKEILKLVETYIS KARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQ SVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPAAFKLFVDAICWAFKH NNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQ ALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFL SALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENA
| ID | Name | Formula | Copies |
|---|---|---|---|
| MPO | 3[N-morpholino]propane sulfonic acid | C7 H15 N O4 S | 1 |
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 1 |
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (DMS, CL, GOL) are not listed.
Novel Mechanistic Observations and NES-Binding Groove Features Revealed by the CRM1 Inhibitors Plumbagin and Oridonin. Lei, Y., Li, Y., Tan, Y. et al. J Nat Prod (2021) 84:1478-1488. DOI 10.1021/acs.jnatprod.0c01231 · 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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