Complex of Transportin 1 with JKTBP NLS. Determined by X-ray diffraction at 3.2 Å resolution. Released 23 Oct 2007.
Explore 2Z5O in 3D Show helices and sheets RCSB PDB PDBe
2Z5O contains 65 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 | 10-21 | 12 | |
| α-helix | 27-33 | 7 | |
| α-helix | 36-39 | 4 | |
| α-helix | 45-55 | 11 | |
| α-helix | 62-76 | 15 | |
| α-helix | 85-97 | 13 | |
| α-helix | 98-100 | 3 | |
| α-helix | 104-121 | 18 | |
| α-helix | 129-137 | 9 | |
| α-helix | 142-164 | 23 | |
| β-strand | 167 | 1 | 1 |
| β-strand | 169 | 1 | 1 |
| α-helix | 172-182 | 11 | |
| 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 | 247-250 | 4 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-284 | 15 | |
| α-helix | 290-293 | 4 | |
| α-helix | 294-296 | 3 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-316 | 5 | |
| 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 | 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 | 516-518 | 3 | |
| α-helix | 519-528 | 10 | |
| α-helix | 529-531 | 3 | |
| α-helix | 536-552 | 17 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-574 | 16 | |
| α-helix | 583-597 | 15 | |
| α-helix | 598-601 | 4 | |
| α-helix | 602-626 | 25 | |
| 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 | 683-702 | 20 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| 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 | 787-789 | 3 | |
| α-helix | 790-801 | 12 | |
| α-helix | 808-823 | 16 | |
| α-helix | 829-831 | 3 | |
| α-helix | 832-840 | 9 | |
| α-helix | 847-859 | 13 | |
| α-helix | 866-872 | 7 | |
| α-helix | 878-888 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A | protein | 890 | Homo sapiens | Q92973 (AlphaFold model) |
| Heterogeneous nuclear ribonucleoprotein D-like | B | protein | 10 |
>2Z5O_1 Transportin-1 (chains A) MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL IPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDD DDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILV LGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKP LMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLI LYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSG FLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIE QLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPE FISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGY VCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVA SWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV
>2Z5O_2 Heterogeneous nuclear ribonucleoprotein D-like (chains B) XXXXXXXXXX
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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