Crystal structure of Transportin-1 in complex with BAP1 PY-NLS (residues 706-724). Determined by X-ray diffraction at 3.76 Å resolution. Released 20 Apr 2022.
Explore 7VPW in 3D Show helices and sheets RCSB PDB PDBe
7VPW contains 70 α-helices and 0 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 | 12-22 | 11 | |
| α-helix | 27-40 | 14 | |
| α-helix | 45-56 | 12 | |
| α-helix | 62-77 | 16 | |
| α-helix | 80-82 | 3 | |
| α-helix | 85-97 | 13 | |
| α-helix | 104-119 | 16 | |
| α-helix | 123-125 | 3 | |
| α-helix | 129-135 | 7 | |
| α-helix | 136-138 | 3 | |
| α-helix | 142-158 | 17 | |
| α-helix | 160-163 | 4 | |
| α-helix | 166-168 | 3 | |
| α-helix | 172-181 | 10 | |
| α-helix | 182-184 | 3 | |
| α-helix | 188-199 | 12 | |
| α-helix | 207-210 | 4 | |
| 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 | 270-284 | 15 | |
| α-helix | 289-292 | 4 | |
| α-helix | 293-295 | 3 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-318 | 7 | |
| α-helix | 375-390 | 16 | |
| α-helix | 391-397 | 7 | |
| α-helix | 399-405 | 7 | |
| α-helix | 411-423 | 13 | |
| α-helix | 425-432 | 8 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-464 | 13 | |
| α-helix | 466-471 | 6 | |
| α-helix | 474-478 | 5 | |
| α-helix | 479-489 | 11 | |
| 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 | 660-663 | 4 | |
| α-helix | 668-675 | 8 | |
| α-helix | 681-697 | 17 | |
| α-helix | 699-702 | 4 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-716 | 11 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-746 | 7 | |
| α-helix | 747-758 | 12 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-792 | 6 | |
| α-helix | 794-801 | 8 | |
| α-helix | 808-821 | 14 | |
| α-helix | 826-829 | 4 | |
| α-helix | 832-840 | 9 | |
| α-helix | 847-864 | 18 | |
| α-helix | 866-873 | 8 | |
| α-helix | 878-888 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| BRCA1-associated protein 1 (BAP1) | B | protein | 19 | Homo sapiens | Q92560 (AlphaFold model) |
| Transportin-1 | A | protein | 870 | Homo sapiens | Q92973 (AlphaFold model) |
>7VPW_1 BRCA1-associated protein 1 (BAP1) (chains B) IGRLHKQRKPDRRKRSRPY
>7VPW_2 Transportin-1 (chains A) GGSKMEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTK LKSEDEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITT IASKGELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMI PKFLQFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVC RALVMLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRH LPKLIPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRGGSGGSGDTISDWNLRKCSA AALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELI PHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAA CSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPE YIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTL AQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKM PEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMG IEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTS LRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGF KNQVGDENWRRFSDQFPLPLKERLAAFYGV
Tumor suppressor BAP1 nuclear import is governed by transportin-1. Yang, T.J., Li, T.N., Huang, R.S. et al. J Cell Biol (2022) 221. DOI 10.1083/jcb.202201094 · PubMed
Other PDB entries of the same protein (UniProt Q92560 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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