Crystal structure of transport factor karyopherin-beta 2 in complex with the PY-NLS of ribosomal protein L4 (RpL4). Determined by X-ray diffraction at 3.0 Å resolution. Released 15 Feb 2017.
Explore 5TQC in 3D Show helices and sheets RCSB PDB PDBe
5TQC contains 67 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 | 27-42 | 16 | |
| α-helix | 47-51 | 5 | |
| α-helix | 52-56 | 5 | |
| α-helix | 62-79 | 18 | |
| α-helix | 85-96 | 12 | |
| α-helix | 104-120 | 17 | |
| α-helix | 123-125 | 3 | |
| α-helix | 130-137 | 8 | |
| α-helix | 142-158 | 17 | |
| α-helix | 160-163 | 4 | |
| α-helix | 172-179 | 8 | |
| α-helix | 180-182 | 3 | |
| α-helix | 188-198 | 11 | |
| α-helix | 199-201 | 3 | |
| α-helix | 207-210 | 4 | |
| α-helix | 213-222 | 10 | |
| α-helix | 229-245 | 17 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-283 | 14 | |
| α-helix | 289-292 | 4 | |
| α-helix | 297-306 | 10 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-318 | 7 | |
| 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 | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-464 | 13 | |
| α-helix | 466-471 | 6 | |
| α-helix | 478-489 | 12 | |
| α-helix | 494-511 | 18 | |
| α-helix | 512-518 | 7 | |
| α-helix | 519-528 | 10 | |
| 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 | 605-628 | 24 | |
| α-helix | 634-636 | 3 | |
| α-helix | 638-655 | 18 | |
| 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 | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 741-746 | 6 | |
| α-helix | 748-759 | 12 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-800 | 11 | |
| α-helix | 808-823 | 16 | |
| α-helix | 826-830 | 5 | |
| α-helix | 832-840 | 9 | |
| α-helix | 847-864 | 18 | |
| α-helix | 867-873 | 7 | |
| α-helix | 878-887 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1,Transportin-1 | A | protein | 866 | Homo sapiens | Q92973 (AlphaFold model) |
| 60S ribosomal protein L4-like protein | B | protein | 26 | Chaetomium thermophilum | G0SFC3 (AlphaFold model) |
>5TQC_1 Transportin-1,Transportin-1 (chains A) MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL IPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIGGSGGSGDDTISDWNLRKCSAAALD VLANVYRDELLPHILPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELIPHLI QCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAACSAF ATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPEYIQM LMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTLAQAM LNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKMPEVR QSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMGIEMQ PYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNI RDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGFKNQV GDENWRRFSDQFPLPLKERLAAFYGV
>5TQC_2 60S ribosomal protein L4-like protein (chains B) SRTKRACVQKKNPLRNKQIMLRLNPY
Molecular basis for protection of ribosomal protein L4 from cellular degradation. Huber, F.M., Hoelz, A. Nat Commun (2017) 8:14354-14354. DOI 10.1038/ncomms14354 · 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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