Crystal structure of Karyopherin beta2 in complex with FUS(456-526). Determined by X-ray diffraction at 2.9 Å resolution. Released 16 May 2018.
Explore 5YVI in 3D Show helices and sheets RCSB PDB PDBe
5YVI contains 68 α-helices and 0 β-strands across 2 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 | 9-21 | 13 | |
| α-helix | 29-40 | 12 | |
| α-helix | 44-55 | 12 | |
| α-helix | 62-79 | 18 | |
| α-helix | 80-82 | 3 | |
| α-helix | 87-96 | 10 | |
| α-helix | 104-119 | 16 | |
| α-helix | 123-125 | 3 | |
| α-helix | 129-137 | 9 | |
| α-helix | 142-159 | 18 | |
| α-helix | 172-179 | 8 | |
| α-helix | 180-184 | 5 | |
| α-helix | 188-199 | 12 | |
| α-helix | 207-210 | 4 | |
| α-helix | 213-222 | 10 | |
| α-helix | 229-245 | 17 | |
| α-helix | 247-250 | 4 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-285 | 16 | |
| α-helix | 289-292 | 4 | |
| α-helix | 293-295 | 3 | |
| α-helix | 297-306 | 10 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-317 | 6 | |
| α-helix | 375-390 | 16 | |
| α-helix | 391-394 | 4 | |
| α-helix | 395-405 | 11 | |
| α-helix | 411-423 | 13 | |
| α-helix | 429-432 | 4 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-463 | 12 | |
| α-helix | 466-471 | 6 | |
| α-helix | 478-489 | 12 | |
| α-helix | 494-511 | 18 | |
| α-helix | 512-518 | 7 | |
| α-helix | 519-532 | 14 | |
| α-helix | 536-552 | 17 | |
| 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 | 668-675 | 8 | |
| α-helix | 681-697 | 17 | |
| α-helix | 699-702 | 4 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-749 | 10 | |
| α-helix | 751-758 | 8 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-801 | 12 | |
| α-helix | 808-819 | 12 | |
| α-helix | 825-827 | 3 | |
| α-helix | 829-831 | 3 | |
| α-helix | 832-840 | 9 | |
| α-helix | 847-861 | 15 | |
| α-helix | 870-873 | 4 | |
| α-helix | 878-888 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 514-521 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A | protein | 868 | Homo sapiens | Q92973 (AlphaFold model) |
| RNA-binding protein FUS | B | protein | 73 | Homo sapiens | P35637 (AlphaFold model) |
>5YVI_1 Transportin-1 (chains A) GSMEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLK SEDEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIA SKGELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPK FLQFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRA LVMLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLP KLIPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRGGSGGSGDTISDWNLRKCSAAA LDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELIPH LIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAACS AFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPEYI QMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTLAQ AMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKMPE VRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMGIE MQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTSLR NIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGFKN QVGDENWRRFSDQFPLPLKERLAAFYGV
>5YVI_2 RNA-binding protein FUS (chains B) GSGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDS RGEHRQDRRERPY
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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