Crystal structure of the biportin Pdr6 in complex with RanGTP. Determined by X-ray diffraction at 2.99 Å resolution. Released 1 May 2019.
Explore 6Q82 in 3D Show helices and sheets RCSB PDB PDBe
6Q82 contains 70 α-helices and 12 β-strands across 2 chains. 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 | 4-14 | 11 | |
| α-helix | 23-33 | 11 | |
| α-helix | 39-48 | 10 | |
| α-helix | 54-63 | 10 | |
| α-helix | 81-98 | 18 | |
| α-helix | 109-125 | 17 | |
| α-helix | 145-150 | 6 | |
| α-helix | 164-170 | 7 | |
| α-helix | 177-183 | 7 | |
| α-helix | 187-210 | 24 | |
| α-helix | 217-220 | 4 | |
| α-helix | 221-225 | 5 | |
| α-helix | 226-238 | 13 | |
| α-helix | 246-261 | 16 | |
| α-helix | 273-284 | 12 | |
| α-helix | 294-309 | 16 | |
| α-helix | 311-313 | 3 | |
| α-helix | 316-327 | 12 | |
| α-helix | 345-355 | 11 | |
| α-helix | 359-373 | 15 | |
| α-helix | 377-385 | 9 | |
| β-strand | 386 | 1 | 1 |
| α-helix | 398-412 | 15 | |
| β-strand | 418 | 1 | 2 |
| β-strand | 422 | 1 | 2 |
| α-helix | 424-427 | 4 | |
| α-helix | 429-440 | 12 | |
| β-strand | 447 | 1 | 1 |
| α-helix | 451-469 | 19 | |
| α-helix | 472-482 | 11 | |
| α-helix | 486-509 | 24 | |
| α-helix | 511-515 | 5 | |
| α-helix | 516-523 | 8 | |
| α-helix | 538-556 | 19 | |
| α-helix | 565-571 | 7 | |
| α-helix | 576-588 | 13 | |
| α-helix | 595-621 | 27 | |
| α-helix | 623-625 | 3 | |
| α-helix | 626-642 | 17 | |
| α-helix | 651-671 | 21 | |
| α-helix | 677-679 | 3 | |
| α-helix | 680-690 | 11 | |
| α-helix | 699-714 | 16 | |
| α-helix | 721-745 | 25 | |
| α-helix | 750-769 | 20 | |
| α-helix | 772-773 | 2 | |
| α-helix | 782-795 | 14 | |
| α-helix | 800-812 | 13 | |
| α-helix | 815-818 | 4 | |
| α-helix | 821-832 | 12 | |
| α-helix | 837-838 | 2 | |
| α-helix | 849-859 | 11 | |
| α-helix | 865-882 | 18 | |
| α-helix | 889-899 | 11 | |
| α-helix | 901-903 | 3 | |
| α-helix | 904-908 | 5 | |
| α-helix | 912-928 | 17 | |
| α-helix | 930-934 | 5 | |
| α-helix | 939-943 | 5 | |
| α-helix | 944-949 | 6 | |
| α-helix | 956-971 | 16 | |
| α-helix | 977-989 | 13 | |
| α-helix | 991-1004 | 14 | |
| α-helix | 1011-1023 | 13 | |
| α-helix | 1025-1035 | 11 | |
| α-helix | 1045-1057 | 13 | |
| α-helix | 1064-1070 | 7 | |
| α-helix | 1072-1075 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-17 | 9 | 3 |
| α-helix | 23-32 | 10 | |
| β-strand | 45-52 | 8 | 3 |
| β-strand | 59-66 | 8 | 3 |
| α-helix | 70-72 | 3 | |
| α-helix | 76-80 | 5 | |
| β-strand | 85-91 | 7 | 3 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-109 | 9 | |
| β-strand | 117-122 | 6 | 3 |
| β-strand | 144-148 | 5 | 3 |
| β-strand | 150 | 1 | 4 |
| β-strand | 155 | 1 | 4 |
| α-helix | 159-169 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin beta-like protein KAP122 | A | protein | 1080 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P32767 (AlphaFold model) |
| GTP-binding nuclear protein Ran | B | protein | 176 | Homo sapiens | P62826 (AlphaFold model) |
>6Q82_1 Importin beta-like protein KAP122 (chains A) SSIHEVVALIEELYSPHPKHDVNQIQQSLQSIQKSEQGFHLANELLSDDKYSANVKYFGA LTLTVQLNTRGENDYETLWNVFRSNLLYLTKFSTLYVSNPNMYGQSLIIIKKLMSNLSLI FTKINDPQLNNAGNENMIKQWNNPINTFIQLMSVQNQNINADQLLLDSINCSLTYEQLSQ FVSLSQKHNELALTFTEVIVEDLTKFQTKRHSMSQIHEVVHEHLYISTMALINLNLTAQA VFNPTVFDCITAWINYISLTRSVSSSGRMDLSEIFQNLIDLMYQSTEGSDGYENAEKILT IFGNVFANDPLLMSYDLRQQIECIFLGVVRPDSGITDISNKNSWMLQYMNYLVTNDFFSE LKELAICIVDFLQINTLSVCNKLFTNIQAADNGQVQDEYIQEYIKVLLQMTNFPLTPVLQ EFFSVRMVDFWLDLSDAYTNLASETLRPNSIELSTQIFQQLINIYLPKISLSVKQRIIEE EGESTSVNEFEDFRNAVSDLAQSLWSILGNDNLTNVLIDGMGQMPAASDETLIIKDTDVL FRIETMCFVLNTILVDMTLSESPWIKNIVDANKFFNQNVISVFQTGFQTSASTKVSQILK LDFVRTSTTLIGTLAGYFKQEPFQLNPYVEALFQGLHTCTNFTSKNEQEKISNDKLEVMV IKTVSTLCETCREELTPYLMHFISFLNTVIMPDSNVSHFTRTKLVRSIGYVVQCQVSNGP EEQAKYILQLTNLLSGSIEHCLASSVQLQEQQDYINCLLYCISELATSLIQPTEIIENDA LLQRLSEFQSFWSSDPLQIRSKIMCTIDKVLDNSIYCKNSAFVEIGCLIVGKGLNLPDGE PYFLKYNMSEVMNFVLRHVPNCELATCLPYFVYLLEKLISEFRKELTPQEFDFMFEKILL VYYDAYIINDPDLLQMTIGFVNNVLDVKPGLAIGSKHWTSFILPQFLKLIPSREKFTIVA VAKFWTKLINNKKYNQEELTTVRQQVSSIGGDLVYQIMYGLFHTQRSDLNSYTDLLRALV AKFPIEAREWLVAVLPQICNNPAGHEKFINKLLITRGSRAAGNVILQWWLDCTTLPNYQG
>6Q82_2 GTP-binding nuclear protein Ran (chains B) GEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVW DTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKV DIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
Structural basis for the nuclear import and export functions of the biportin Pdr6/Kap122. Aksu, M., Trakhanov, S., Vera Rodriguez, A. et al. J Cell Biol (2019) 218:1839-1852. DOI 10.1083/jcb.201812093 · PubMed
Other PDB entries of the same protein (UniProt P32767 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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