Crystal structure of KPT276 in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 1.8 Å resolution. Released 15 Jul 2015.
Explore 4WVF in 3D Show helices and sheets RCSB PDB PDBe
4WVF contains 86 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 | 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 | 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 | 188-190 | 3 | |
| α-helix | 191-193 | 3 | |
| α-helix | 194-205 | 12 | |
| α-helix | 208-209 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 66-68 | 3 | |
| 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 | 170-178 | 9 | 2 |
| α-helix | 181-199 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-5 | 6 | |
| α-helix | 13-25 | 13 | |
| α-helix | 28-43 | 16 | |
| α-helix | 47-50 | 4 | |
| α-helix | 51-57 | 7 | |
| α-helix | 61-78 | 18 | |
| 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 | 176-202 | 27 | |
| α-helix | 208-220 | 13 | |
| α-helix | 227-230 | 4 | |
| α-helix | 234-239 | 6 | |
| α-helix | 241-244 | 4 | |
| α-helix | 246-259 | 14 | |
| α-helix | 269-285 | 17 | |
| α-helix | 286-290 | 5 | |
| α-helix | 297-303 | 7 | |
| α-helix | 308-326 | 19 | |
| α-helix | 328-331 | 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 | 435-438 | 4 | |
| β-strand | 443-445 | 3 | 3 |
| β-strand | 451-453 | 3 | 3 |
| α-helix | 459-461 | 3 | |
| α-helix | 462-478 | 17 | |
| α-helix | 480-495 | 16 | |
| α-helix | 502-514 | 13 | |
| α-helix | 521-541 | 21 | |
| α-helix | 544-560 | 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 | 629-632 | 4 | |
| α-helix | 638-652 | 15 | |
| α-helix | 658-668 | 11 | |
| α-helix | 670-685 | 16 | |
| α-helix | 688-691 | 4 | |
| 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 | 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTP-binding nuclear protein Ran | A | protein | 216 | Homo sapiens | P62826 (AlphaFold model) |
| Ran-specific GTPase-activating protein 1 | B | protein | 140 | Saccharomyces cerevisiae | P41920 (AlphaFold model) |
| Crm1p | C | protein | 1024 | Saccharomyces cerevisiae | P30822 (AlphaFold model) |
>4WVF_1 GTP-binding nuclear protein Ran (chains A) MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
>4WVF_2 Ran-specific GTPase-activating protein 1 (chains B) DIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKKTNK VRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRFGSK ENADKFKEEFEKAQEINKKA
>4WVF_3 Crm1p (chains C) GGSMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQF STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVRE FVKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGS ISGTMSEDTEKRFVVTVIKDLLDLCVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLR TVILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTA DLQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSE TVKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTP KVRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNC MTTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAF LELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFI FVSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQY LANMLSNAFPHLTSEQIASFLSALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAED KENA
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
| K76 | (2E)-3-{3-[3,5-bis(trifluoromethyl)phenyl]-1H-1,2,4-triazol-1-yl}-1-(3,3-difluo… | C16 H10 F8 N4 O | 1 |
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 1 |
Water and common crystallization additives (GOL, CL, EDO) are not listed.
Nuclear export inhibitors avert progression in preclinical models of inflammatory demyelination. Haines, J.D., Herbin, O., de la Hera, B. et al. Nat Neurosci (2015) 18:511-520. DOI 10.1038/nn.3953 · 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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