Crystal structure of unliganded Saccharomyces cerevisiae CRM1 (Xpo1p). Determined by X-ray diffraction at 2.1 Å resolution. Released 28 Nov 2012.
Explore 3VYC in 3D Show helices and sheets RCSB PDB PDBe
3VYC contains 65 α-helices and 2 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 51-55 | 5 | |
| α-helix | 67-75 | 9 | |
| α-helix | 84-103 | 20 | |
| α-helix | 105-109 | 5 | |
| α-helix | 112-129 | 18 | |
| α-helix | 137-146 | 10 | |
| α-helix | 149-162 | 14 | |
| α-helix | 163-167 | 5 | |
| α-helix | 177-185 | 9 | |
| α-helix | 187-202 | 16 | |
| α-helix | 207-220 | 14 | |
| α-helix | 227-230 | 4 | |
| α-helix | 234-237 | 4 | |
| α-helix | 238-242 | 5 | |
| α-helix | 243-244 | 2 | |
| α-helix | 246-259 | 14 | |
| α-helix | 272-289 | 18 | |
| α-helix | 297-303 | 7 | |
| α-helix | 306-332 | 27 | |
| α-helix | 337-350 | 14 | |
| α-helix | 356-375 | 20 | |
| α-helix | 414-420 | 7 | |
| α-helix | 421-432 | 12 | |
| α-helix | 435-438 | 4 | |
| β-strand | 443-445 | 3 | 1 |
| β-strand | 451-453 | 3 | 1 |
| α-helix | 459-478 | 20 | |
| 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 | 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 | 687-691 | 5 | |
| α-helix | 693-713 | 21 | |
| α-helix | 714-717 | 4 | |
| α-helix | 718-745 | 28 | |
| 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 | 879-894 | 16 | |
| α-helix | 898-918 | 21 | |
| α-helix | 922-927 | 6 | |
| α-helix | 928-932 | 5 | |
| α-helix | 933-944 | 12 | |
| α-helix | 952-967 | 16 | |
| α-helix | 988-1002 | 15 | |
| α-helix | 1008-1019 | 12 | |
| α-helix | 1025-1043 | 19 | |
| α-helix | 1049-1070 | 22 | |
| α-helix | 1079-1081 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Exportin-1 | A | protein | 1033 | Saccharomyces cerevisiae | P30822 (AlphaFold model) |
>3VYC_1 Exportin-1 (chains A) MEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFSTN PQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKSDL TLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQAKAL HLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELLST KFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLKAT YANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERELFK TTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREFVK ESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISG TMSEDTEKRFVVTVIKDLLDLTVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRTVI LKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQ PQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVK IIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVR GLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTT VVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLEL PPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVS ETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKTSNQVYLSQYLANMLSNAFPHLTSEQI ASFLSALTKQYKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENALMEQNRLEREKAA KIGGLLKPSELDD
A 2.1- angstrom -resolution crystal structure of unliganded CRM1 reveals the mechanism of autoinhibition. Saito, N., Matsuura, Y. J Mol Biol (2013) 425:350-364. DOI 10.1016/j.jmb.2012.11.014 · PubMed
Other PDB entries of the same protein (UniProt P30822 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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