Complex of Transportin 1 with TAP NLS. Determined by X-ray diffraction at 2.6 Å resolution. Released 23 Oct 2007.
Explore 2Z5K in 3D Show helices and sheets RCSB PDB PDBe
2Z5K contains 67 α-helices and 2 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 | 9-20 | 12 | |
| α-helix | 21-23 | 3 | |
| α-helix | 27-38 | 12 | |
| α-helix | 39-42 | 4 | |
| α-helix | 46-55 | 10 | |
| α-helix | 62-77 | 16 | |
| α-helix | 85-96 | 12 | |
| α-helix | 104-120 | 17 | |
| α-helix | 129-136 | 8 | |
| α-helix | 142-158 | 17 | |
| α-helix | 160-164 | 5 | |
| β-strand | 167 | 1 | 1 |
| β-strand | 169 | 1 | 1 |
| α-helix | 172-181 | 10 | |
| α-helix | 182-184 | 3 | |
| α-helix | 188-198 | 11 | |
| α-helix | 199-201 | 3 | |
| α-helix | 207-210 | 4 | |
| α-helix | 213-223 | 11 | |
| α-helix | 229-245 | 17 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-285 | 16 | |
| α-helix | 289-292 | 4 | |
| α-helix | 294-296 | 3 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-318 | 7 | |
| α-helix | 375-390 | 16 | |
| α-helix | 391-394 | 4 | |
| α-helix | 395-406 | 12 | |
| 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 | 478-489 | 12 | |
| α-helix | 494-511 | 18 | |
| α-helix | 512-518 | 7 | |
| α-helix | 519-530 | 12 | |
| α-helix | 536-552 | 17 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-575 | 17 | |
| α-helix | 583-597 | 15 | |
| α-helix | 598-601 | 4 | |
| α-helix | 602-627 | 26 | |
| 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 | 706-714 | 9 | |
| 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 | 790-801 | 12 | |
| 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) |
| Nuclear RNA export factor 1 | B | protein | 30 | Homo sapiens | Q9UBU9 (AlphaFold model) |
>2Z5K_1 Transportin-1 (chains A) MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL IPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDD DDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILV LGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKP LMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLI LYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSG FLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIE QLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPE FISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGY VCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVA SWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV
>2Z5K_2 Nuclear RNA export factor 1 (chains B) EEDDGDVAMSDAQDGPRVRYNPYTTRPNRR
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 1 |
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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