Crystal Structure of SMAD4 NES Peptide in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 2.24 Å resolution. Released 22 Mar 2017.
Explore 5UWU in 3D Show helices and sheets RCSB PDB PDBe
5UWU contains 87 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 | 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 | 182-187 | 6 | |
| 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 | 147-149 | 3 | 2 |
| β-strand | 152-163 | 12 | 2 |
| β-strand | 170-177 | 8 | 2 |
| α-helix | 181-199 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1-5 | 5 | |
| α-helix | 10-11 | 2 | |
| α-helix | 13-25 | 13 | |
| α-helix | 28-42 | 15 | |
| 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 | 137-145 | 9 | |
| α-helix | 149-163 | 15 | |
| α-helix | 164-168 | 5 | |
| α-helix | 176-188 | 13 | |
| α-helix | 190-203 | 14 | |
| α-helix | 207-220 | 14 | |
| α-helix | 227-230 | 4 | |
| α-helix | 234-239 | 6 | |
| α-helix | 241-244 | 4 | |
| α-helix | 246-259 | 14 | |
| α-helix | 269-289 | 21 | |
| 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 | 435-437 | 3 | |
| α-helix | 462-478 | 17 | |
| α-helix | 480-495 | 16 | |
| α-helix | 502-514 | 13 | |
| α-helix | 521-541 | 21 | |
| α-helix | 545-560 | 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 | 638-652 | 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 | 783-788 | 6 | |
| α-helix | 789-800 | 12 | |
| 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 | 922-927 | 6 | |
| α-helix | 928-932 | 5 | |
| α-helix | 933-944 | 12 | |
| 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 | 143-145 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTP-binding nuclear protein Ran | A | protein | 237 | Homo sapiens | P62826 (AlphaFold model) |
| Ran-specific GTPase-activating protein 1 | B | protein | 143 | Saccharomyces cerevisiae | P41920 (AlphaFold model) |
| Exportin-1 | C | protein | 1024 | Saccharomyces cerevisiae | P30822 (AlphaFold model) |
| Mothers against decapentaplegic homolog 4 | D | protein | 20 | Homo sapiens | Q13485 (AlphaFold model) |
>5UWU_1 GTP-binding nuclear protein Ran (chains A) METGSSHHHHHHSSGLPRGSHMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKY VATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYK NVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEK PFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
>5UWU_2 Ran-specific GTPase-activating protein 1 (chains B) GGSDIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKK TNKVRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRF GSKENADKFKEEFEKAQEINKKA
>5UWU_3 Exportin-1 (chains C) GGSMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQF STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEDLVVENDEGEIVRE FVKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGS ISGTMSEDTEKRFVVTVIKDLLGLCEQKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLR TVILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTA DLQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSE TVKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTP KVRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNC MTTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAF LELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFI FVSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQY LANMLSNAFPHLTSEQIASFLSALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAED KENA
>5UWU_4 Mothers against decapentaplegic homolog 4 (chains D) GGSYERVVSPGIDLSGLTLQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 1 |
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (GOL, CL) are not listed.
Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals. Fung, H.Y., Fu, S.C., Chook, Y.M. Elife (2017) 6. DOI 10.7554/eLife.23961 · 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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