Complex of Transportin 1 with hnRNP D NLS. Determined by X-ray diffraction at 3.2 Å resolution. Released 23 Oct 2007.
Explore 2Z5N in 3D Show helices and sheets RCSB PDB PDBe
2Z5N contains 63 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 | 15-20 | 6 | |
| α-helix | 27-38 | 12 | |
| α-helix | 39-42 | 4 | |
| α-helix | 46-55 | 10 | |
| α-helix | 62-77 | 16 | |
| α-helix | 85-97 | 13 | |
| α-helix | 98-100 | 3 | |
| α-helix | 104-120 | 17 | |
| α-helix | 129-133 | 5 | |
| α-helix | 142-158 | 17 | |
| α-helix | 176-181 | 6 | |
| α-helix | 182-184 | 3 | |
| α-helix | 188-199 | 12 | |
| α-helix | 207-210 | 4 | |
| α-helix | 215-221 | 7 | |
| α-helix | 229-241 | 13 | |
| α-helix | 247-249 | 3 | |
| α-helix | 254-264 | 11 | |
| α-helix | 270-283 | 14 | |
| α-helix | 287-291 | 5 | |
| α-helix | 293-305 | 13 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-316 | 5 | |
| α-helix | 375-390 | 16 | |
| α-helix | 395-397 | 3 | |
| α-helix | 399-406 | 8 | |
| α-helix | 411-423 | 13 | |
| α-helix | 430-435 | 6 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-463 | 12 | |
| α-helix | 466-471 | 6 | |
| α-helix | 478-489 | 12 | |
| α-helix | 494-510 | 17 | |
| α-helix | 516-518 | 3 | |
| α-helix | 519-528 | 10 | |
| α-helix | 529-531 | 3 | |
| α-helix | 535-552 | 18 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-574 | 16 | |
| α-helix | 583-596 | 14 | |
| α-helix | 605-627 | 23 | |
| α-helix | 634-637 | 4 | |
| α-helix | 639-655 | 17 | |
| α-helix | 656-658 | 3 | |
| α-helix | 660-664 | 5 | |
| α-helix | 669-675 | 7 | |
| α-helix | 681-697 | 17 | |
| α-helix | 699-701 | 3 | |
| α-helix | 706-715 | 10 | |
| 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 | 796-801 | 6 | |
| α-helix | 808-823 | 16 | |
| α-helix | 825-827 | 3 | |
| α-helix | 829-831 | 3 | |
| α-helix | 832-840 | 9 | |
| α-helix | 847-864 | 18 | |
| α-helix | 866-873 | 8 | |
| α-helix | 878-887 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A | protein | 890 | Homo sapiens | Q92973 (AlphaFold model) |
| Heterogeneous nuclear ribonucleoprotein D0 | B | protein | 24 | Q14103 (AlphaFold model) |
>2Z5N_1 Transportin-1 (chains A) MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL IPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDD DDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILV LGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKP LMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLI LYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSG FLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIE QLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPE FISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGY VCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVA SWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV
>2Z5N_2 Heterogeneous nuclear ribonucleoprotein D0 (chains B) YSNQQSGYGKVSRRGGHQNSYKPY
Structural basis for substrate recognition and dissociation by human transportin 1. Imasaki, T., Shimizu, T., Hashimoto, H. et al. Mol Cell (2007) 28:57-67. DOI 10.1016/j.molcel.2007.08.006 · 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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