Crystal structure of Karyopherin beta2 in complex with FUS(full length). Determined by X-ray diffraction at 4.05 Å resolution. Released 16 May 2018.
Explore 5YVG in 3D Show helices and sheets RCSB PDB PDBe
5YVG contains 117 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 11-20 | 10 | |
| α-helix | 27-39 | 13 | |
| α-helix | 46-55 | 10 | |
| α-helix | 62-77 | 16 | |
| α-helix | 85-97 | 13 | |
| α-helix | 104-121 | 18 | |
| α-helix | 129-136 | 8 | |
| α-helix | 143-158 | 16 | |
| α-helix | 161-163 | 3 | |
| α-helix | 172-181 | 10 | |
| α-helix | 188-198 | 11 | |
| α-helix | 214-220 | 7 | |
| α-helix | 221-225 | 5 | |
| α-helix | 229-244 | 16 | |
| α-helix | 254-264 | 11 | |
| α-helix | 270-275 | 6 | |
| α-helix | 278-285 | 8 | |
| α-helix | 287-291 | 5 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-316 | 5 | |
| α-helix | 375-390 | 16 | |
| α-helix | 395-405 | 11 | |
| α-helix | 411-423 | 13 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-463 | 12 | |
| α-helix | 466-470 | 5 | |
| α-helix | 474-478 | 5 | |
| α-helix | 479-489 | 11 | |
| α-helix | 494-511 | 18 | |
| α-helix | 512-515 | 4 | |
| α-helix | 519-532 | 14 | |
| α-helix | 538-552 | 15 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-575 | 17 | |
| α-helix | 583-597 | 15 | |
| α-helix | 598-604 | 7 | |
| α-helix | 605-628 | 24 | |
| α-helix | 634-636 | 3 | |
| α-helix | 639-655 | 17 | |
| α-helix | 656-659 | 4 | |
| α-helix | 660-664 | 5 | |
| α-helix | 669-675 | 7 | |
| α-helix | 681-697 | 17 | |
| α-helix | 703-715 | 13 | |
| α-helix | 719-721 | 3 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-743 | 4 | |
| α-helix | 747-758 | 12 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-800 | 11 | |
| α-helix | 809-823 | 15 | |
| α-helix | 829-831 | 3 | |
| α-helix | 832-839 | 8 | |
| α-helix | 847-862 | 16 | |
| α-helix | 869-873 | 5 | |
| α-helix | 878-887 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-20 | 9 | |
| α-helix | 28-37 | 10 | |
| α-helix | 51-55 | 5 | |
| α-helix | 62-78 | 17 | |
| α-helix | 88-98 | 11 | |
| α-helix | 106-117 | 12 | |
| α-helix | 129-136 | 8 | |
| α-helix | 146-157 | 12 | |
| α-helix | 175-181 | 7 | |
| α-helix | 189-198 | 10 | |
| α-helix | 214-220 | 7 | |
| α-helix | 221-223 | 3 | |
| α-helix | 229-244 | 16 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-284 | 15 | |
| α-helix | 287-290 | 4 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 375-388 | 14 | |
| α-helix | 400-405 | 6 | |
| α-helix | 411-423 | 13 | |
| α-helix | 430-435 | 6 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-464 | 13 | |
| α-helix | 478-489 | 12 | |
| α-helix | 494-511 | 18 | |
| α-helix | 512-515 | 4 | |
| α-helix | 519-530 | 12 | |
| α-helix | 538-551 | 14 | |
| α-helix | 561-575 | 15 | |
| α-helix | 583-597 | 15 | |
| α-helix | 598-604 | 7 | |
| α-helix | 605-628 | 24 | |
| α-helix | 634-636 | 3 | |
| α-helix | 639-655 | 17 | |
| α-helix | 656-659 | 4 | |
| α-helix | 660-664 | 5 | |
| α-helix | 669-675 | 7 | |
| α-helix | 681-697 | 17 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 719-721 | 3 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-743 | 4 | |
| α-helix | 747-758 | 12 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-800 | 11 | |
| α-helix | 808-823 | 16 | |
| α-helix | 829-831 | 3 | |
| α-helix | 832-839 | 8 | |
| α-helix | 847-861 | 15 | |
| α-helix | 868-873 | 6 | |
| α-helix | 878-887 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 513-520 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 515-520 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A, B | protein | 868 | Homo sapiens | Q92973 (AlphaFold model) |
| RNA-binding protein FUS | X, Y | protein | 528 | Homo sapiens | P35637 (AlphaFold model) |
>5YVG_1 Transportin-1 (chains A, B) GSMEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLK SEDEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIA SKGELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPK FLQFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRA LVMLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLP KLIPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRGGSGGSGDTISDWNLRKCSAAA LDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELIPH LIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAACS AFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPEYI QMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTLAQ AMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKMPE VRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMGIE MQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTSLR NIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGFKN QVGDENWRRFSDQFPLPLKERLAAFYGV
>5YVG_2 RNA-binding protein FUS (chains X, Y) GSMASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSY GQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQ SSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYG QDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGG YEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTI ESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKE FSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGG GQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGG YDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY
Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. Yoshizawa, T., Ali, R., Jiou, J. et al. Cell (2018) 173:693-705.e22. DOI 10.1016/j.cell.2018.03.003 · PubMed
Other PDB entries of the same protein (UniProt Q92973 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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