Free Transportin 1. Determined by X-ray diffraction at 3.4 Å resolution. Released 23 Oct 2007.
Explore 2Z5J in 3D Show helices and sheets RCSB PDB PDBe
2Z5J contains 59 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 | 9-20 | 12 | |
| α-helix | 30-38 | 9 | |
| α-helix | 45-54 | 10 | |
| α-helix | 62-76 | 15 | |
| α-helix | 85-96 | 12 | |
| α-helix | 104-120 | 17 | |
| α-helix | 129-137 | 9 | |
| α-helix | 143-158 | 16 | |
| α-helix | 160-163 | 4 | |
| α-helix | 172-180 | 9 | |
| 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 | 254-264 | 11 | |
| α-helix | 270-283 | 14 | |
| α-helix | 291-294 | 4 | |
| α-helix | 297-308 | 12 | |
| α-helix | 375-390 | 16 | |
| α-helix | 391-397 | 7 | |
| α-helix | 399-404 | 6 | |
| α-helix | 413-423 | 11 | |
| α-helix | 429-432 | 4 | |
| α-helix | 436-446 | 11 | |
| α-helix | 454-463 | 10 | |
| α-helix | 466-469 | 4 | |
| α-helix | 474-487 | 14 | |
| α-helix | 494-511 | 18 | |
| α-helix | 519-529 | 11 | |
| α-helix | 530-532 | 3 | |
| α-helix | 535-552 | 18 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-574 | 16 | |
| α-helix | 583-596 | 14 | |
| α-helix | 598-604 | 7 | |
| α-helix | 605-626 | 22 | |
| α-helix | 634-635 | 2 | |
| α-helix | 639-654 | 16 | |
| α-helix | 656-659 | 4 | |
| α-helix | 660-664 | 5 | |
| α-helix | 668-675 | 8 | |
| α-helix | 681-702 | 22 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-743 | 4 | |
| α-helix | 747-759 | 13 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-801 | 12 | |
| α-helix | 808-821 | 14 | |
| α-helix | 825-827 | 3 | |
| α-helix | 832-839 | 8 | |
| α-helix | 848-864 | 17 | |
| α-helix | 870-873 | 4 | |
| α-helix | 878-887 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A | protein | 890 | Homo sapiens | Q92973 (AlphaFold model) |
>2Z5J_1 Transportin-1 (chains A) MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL IPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDD DDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILV LGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKP LMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLI LYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSG FLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIE QLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPE FISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGY VCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVA SWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV
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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