Crystal structure of transportin/FUS-NLS. Determined by X-ray diffraction at 3.0 Å resolution. Released 21 Aug 2013.
Explore 4FQ3 in 3D Show helices and sheets RCSB PDB PDBe
4FQ3 contains 60 α-helices and 3 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 | 11-22 | 12 | |
| α-helix | 27-40 | 14 | |
| α-helix | 44-51 | 8 | |
| α-helix | 52-56 | 5 | |
| α-helix | 62-77 | 16 | |
| α-helix | 86-97 | 12 | |
| α-helix | 104-120 | 17 | |
| α-helix | 129-137 | 9 | |
| α-helix | 142-158 | 17 | |
| α-helix | 161-164 | 4 | |
| β-strand | 167 | 1 | 1 |
| β-strand | 169 | 1 | 1 |
| α-helix | 172-181 | 10 | |
| α-helix | 188-199 | 12 | |
| α-helix | 207-211 | 5 | |
| α-helix | 213-223 | 11 | |
| α-helix | 229-245 | 17 | |
| α-helix | 247-250 | 4 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-283 | 14 | |
| α-helix | 289-292 | 4 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-317 | 6 | |
| α-helix | 375-390 | 16 | |
| α-helix | 391-394 | 4 | |
| α-helix | 395-406 | 12 | |
| α-helix | 411-432 | 22 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-471 | 20 | |
| α-helix | 478-489 | 12 | |
| α-helix | 494-510 | 17 | |
| α-helix | 516-518 | 3 | |
| α-helix | 519-532 | 14 | |
| α-helix | 538-552 | 15 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-574 | 16 | |
| α-helix | 583-597 | 15 | |
| α-helix | 598-601 | 4 | |
| α-helix | 602-628 | 27 | |
| α-helix | 639-652 | 14 | |
| α-helix | 660-663 | 4 | |
| α-helix | 668-675 | 8 | |
| α-helix | 681-697 | 17 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-743 | 4 | |
| α-helix | 751-758 | 8 | |
| α-helix | 765-781 | 17 | |
| α-helix | 795-801 | 7 | |
| α-helix | 805 | 1 | |
| β-strand | 807 | 1 | 2 |
| α-helix | 808-823 | 16 | |
| α-helix | 825-829 | 5 | |
| α-helix | 833-839 | 7 | |
| α-helix | 847-864 | 18 | |
| α-helix | 870-873 | 4 | |
| α-helix | 878-883 | 6 | |
| α-helix | 884-888 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 514-520 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A | protein | 890 | Homo sapiens | Q92973 (AlphaFold model) |
| Fusion (Involved in t(12;16) in malignant liposarcoma) | B | protein | 37 | Homo sapiens | P35637 (AlphaFold model) |
>4FQ3_1 Transportin-1 (chains A) MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL IPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDD DDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILV LGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKP LMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLI LYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSG FLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIE QLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPE FISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGY VCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVA SWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV
>4FQ3_2 Fusion (Involved in t(12;16) in malignant liposarcoma) (chains B) GPLGSRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY
Crystal structure of transportin/FUS-NLS. Gong, W., Niu, C., Jia, M. et al. To be published.
Other PDB entries of the same protein (UniProt Q92973 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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