Crystal structure of the biportin Pdr6 in complex with UBC9. Determined by X-ray diffraction at 4.53 Å resolution. Released 1 May 2019.
Explore 6Q83 in 3D Show helices and sheets RCSB PDB PDBe
6Q83 contains 71 α-helices and 13 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 | 54-65 | 12 | |
| α-helix | 80-99 | 20 | |
| α-helix | 108-125 | 18 | |
| α-helix | 145-151 | 7 | |
| α-helix | 166-172 | 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 | 273-285 | 13 | |
| α-helix | 294-309 | 16 | |
| α-helix | 311-313 | 3 | |
| α-helix | 316-326 | 11 | |
| α-helix | 345-355 | 11 | |
| α-helix | 359-373 | 15 | |
| α-helix | 378-385 | 8 | |
| β-strand | 386 | 1 | 1 |
| α-helix | 397-413 | 17 | |
| β-strand | 418 | 1 | 2 |
| β-strand | 422 | 1 | 2 |
| α-helix | 424-440 | 17 | |
| α-helix | 444-446 | 3 | |
| β-strand | 447 | 1 | 1 |
| α-helix | 451-466 | 16 | |
| α-helix | 472-481 | 10 | |
| α-helix | 486-510 | 25 | |
| 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 | 595-614 | 20 | |
| α-helix | 616-621 | 6 | |
| α-helix | 623-625 | 3 | |
| α-helix | 627-639 | 13 | |
| α-helix | 650-671 | 22 | |
| 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 | 787-795 | 9 | |
| α-helix | 800-812 | 13 | |
| α-helix | 815-818 | 4 | |
| α-helix | 821-831 | 11 | |
| α-helix | 837-838 | 2 | |
| α-helix | 849-859 | 11 | |
| α-helix | 865-882 | 18 | |
| α-helix | 889-895 | 7 | |
| α-helix | 896-901 | 6 | |
| 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 | 977-1004 | 28 | |
| α-helix | 1012-1023 | 12 | |
| α-helix | 1025-1038 | 14 | |
| α-helix | 1045-1047 | 3 | |
| α-helix | 1048-1055 | 8 | |
| α-helix | 1064-1075 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-18 | 16 | |
| β-strand | 25-30 | 6 | 3 |
| β-strand | 36-46 | 11 | 3 |
| α-helix | 47-48 | 2 | |
| β-strand | 56 | 1 | 4 |
| β-strand | 57-63 | 7 | 3 |
| α-helix | 72-73 | 2 | |
| β-strand | 74-76 | 3 | 3 |
| α-helix | 77-78 | 2 | |
| β-strand | 86 | 1 | 5 |
| β-strand | 91 | 1 | 3 |
| β-strand | 92 | 1 | 5 |
| α-helix | 95-97 | 3 | |
| α-helix | 109-121 | 13 | |
| α-helix | 131-139 | 9 | |
| α-helix | 141-154 | 14 | |
| β-strand | 156 | 1 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin beta-like protein KAP122 | A | protein | 1080 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P32767 (AlphaFold model) |
| UBC9 | B | protein | 157 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P50623 (AlphaFold model) |
>6Q83_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
>6Q83_2 UBC9 (chains B) GSSLCLQRLQEERKKWRKDHPFGFYAKPVKKADGSMDLQKWEAGIPGKEGTNWAGGVYPI TVEYPNEYPSKPPKVKFPAGFYHPNVYPSGTICLSILNEDQDWRPAITLKQIVLGVQDLL DSPNPNSPAQEPAWRSFSRNKAEYDKKVLLQAKQYSK
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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