Crystal structure of human Karyopherin-beta2 bound to the PY-NLS of Saccharomyces cerevisiae NAB2. Determined by X-ray diffraction at 3.05 Å resolution. Released 3 Apr 2013.
Explore 4JLQ in 3D Show helices and sheets RCSB PDB PDBe
4JLQ contains 64 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 | 9-22 | 14 | |
| α-helix | 27-41 | 15 | |
| α-helix | 46-55 | 10 | |
| α-helix | 62-77 | 16 | |
| α-helix | 85-97 | 13 | |
| α-helix | 104-120 | 17 | |
| α-helix | 129-137 | 9 | |
| α-helix | 142-163 | 22 | |
| 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 | 213-221 | 9 | |
| 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 | 289-294 | 6 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-317 | 6 | |
| α-helix | 375-389 | 15 | |
| α-helix | 391-394 | 4 | |
| α-helix | 395-407 | 13 | |
| α-helix | 411-424 | 14 | |
| α-helix | 429-432 | 4 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-464 | 13 | |
| α-helix | 466-470 | 5 | |
| α-helix | 474-478 | 5 | |
| α-helix | 479-488 | 10 | |
| 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 | 577 | 1 | |
| α-helix | 583-597 | 15 | |
| α-helix | 598-604 | 7 | |
| α-helix | 606-628 | 23 | |
| α-helix | 638-654 | 17 | |
| α-helix | 656-659 | 4 | |
| α-helix | 660-664 | 5 | |
| α-helix | 668-675 | 8 | |
| α-helix | 681-698 | 18 | |
| α-helix | 699-701 | 3 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-743 | 4 | |
| α-helix | 748-759 | 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 | 827-830 | 4 | |
| α-helix | 832-839 | 8 | |
| α-helix | 847-873 | 27 | |
| α-helix | 878-887 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A | protein | 854 | Homo sapiens | Q92973 (AlphaFold model) |
| Nuclear polyadenylated RNA-binding protein NAB2 | B | protein | 38 | Saccharomyces cerevisiae S288c | P32505 (AlphaFold model) |
>4JLQ_1 Transportin-1 (chains A) MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL IPVLVNGMKYSDIDIILLKGDVEGGSGGSGDDTISDWNLRKCSAAALDVLANVYRDELLP HILPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRS ITCWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAACSAFATLEEEACTELV PYLAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNML KDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAP DKDFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTK ACFQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVE IINRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRG ICTMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQF PLPLKERLAAFYGV
>4JLQ_2 Nuclear polyadenylated RNA-binding protein NAB2 (chains B) RFTQRGGGAVGKNRRGGRGGNRGGRNNNSTRFNPLAKA
Crystal structure of human Karyopherin beta 2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2. Soniat, M., Sampathkumar, P., Collett, G. et al. J Struct Funct Genomics (2013) 14:31-35. DOI 10.1007/s10969-013-9150-1 · 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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