Crystal structure of Kap114p. Determined by X-ray diffraction at 2.5 Å resolution. Released 23 Oct 2019.
Explore 6AHO in 3D Show helices and sheets RCSB PDB PDBe
6AHO contains 59 α-helices and 6 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 | 3-8 | 6 | |
| α-helix | 16-31 | 16 | |
| α-helix | 34-45 | 12 | |
| α-helix | 51-68 | 18 | |
| α-helix | 84-98 | 15 | |
| α-helix | 105-126 | 22 | |
| α-helix | 130-140 | 11 | |
| α-helix | 144-157 | 14 | |
| α-helix | 160-164 | 5 | |
| α-helix | 168-180 | 13 | |
| α-helix | 187-205 | 19 | |
| α-helix | 213-215 | 3 | |
| α-helix | 216-233 | 18 | |
| α-helix | 243-263 | 21 | |
| α-helix | 266-268 | 3 | |
| α-helix | 271-289 | 19 | |
| α-helix | 304-320 | 17 | |
| α-helix | 328-341 | 14 | |
| α-helix | 344-345 | 2 | |
| α-helix | 346-354 | 9 | |
| α-helix | 356-363 | 8 | |
| α-helix | 372-380 | 9 | |
| α-helix | 385-400 | 16 | |
| α-helix | 409-420 | 12 | |
| α-helix | 431-447 | 17 | |
| α-helix | 453-469 | 17 | |
| α-helix | 471-473 | 3 | |
| α-helix | 477-494 | 18 | |
| α-helix | 498-514 | 17 | |
| α-helix | 517-520 | 4 | |
| α-helix | 523-541 | 19 | |
| α-helix | 546-561 | 16 | |
| α-helix | 571-587 | 17 | |
| α-helix | 592-605 | 14 | |
| α-helix | 611-634 | 24 | |
| α-helix | 641-654 | 14 | |
| α-helix | 662 | 1 | |
| β-strand | 663 | 1 | 1 |
| α-helix | 664 | 1 | |
| α-helix | 665-681 | 17 | |
| α-helix | 685-700 | 16 | |
| β-strand | 702 | 1 | 1 |
| α-helix | 704-707 | 4 | |
| α-helix | 708-710 | 3 | |
| α-helix | 711-722 | 12 | |
| α-helix | 728-731 | 4 | |
| α-helix | 735-744 | 10 | |
| α-helix | 746-749 | 4 | |
| α-helix | 750-752 | 3 | |
| α-helix | 753-766 | 14 | |
| α-helix | 770-786 | 17 | |
| α-helix | 788-795 | 8 | |
| β-strand | 799-800 | 2 | 2 |
| β-strand | 803-804 | 2 | 2 |
| α-helix | 805-817 | 13 | |
| α-helix | 823-837 | 15 | |
| α-helix | 842-846 | 5 | |
| β-strand | 848-854 | 7 | 3 |
| β-strand | 873-878 | 6 | 3 |
| α-helix | 879-895 | 17 | |
| α-helix | 897-899 | 3 | |
| α-helix | 965-979 | 15 | |
| α-helix | 981-983 | 3 | |
| α-helix | 984-990 | 7 | |
| α-helix | 993-1002 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-5 | A | protein | 1009 | Saccharomyces cerevisiae | P53067 (AlphaFold model) |
>6AHO_1 Importin subunit beta-5 (chains A) GPLGSMDINELIIGAQSADKHTREVAETQLLQWCDSDASQVFKALANVALQHEASLESRQ FALLSLRKLITMYWSPGFESYRSTSNVEIDVKDFIREVLLKLCLNDNENTKIKNGASYCI VQISAVDFPDQWPQLLTVIYDAISHQHSLNAMSLLNEIYDDVVSEEMFFEGGIGLATMEI VFKVLNTETSTLIAKIAALKLLKACLLQMSSHNEYDEASRKSFVSQCLATSLQILGQLLT LNFGNVDVISQLKFKSIIYENLVFIKNDFSRKHFSSELQKQFKIMAIQDLENVTHINANV ETTESEPLLETVHDCSIYIVEFLTSVCTLQFSVEEMNKIITSLTILCQLSSETREIWTSD FNTFVSKETGLAASYNVRDQANEFFTSLPNPQLSLIFKVVSNDIEHSTCNYSTLESLLYL LQCILLNDDEITGENIDQSLQILIKTLENILVSQEIPELILARAILTIPRVLDKFIDALP DIKPLTSAFLAKSLNLALKSDKELIKSATLIAFTYYCYFAELDSVLGPEVCSETQEKVIR IINQVSSDAEEDTNGALMEVLSQVISYNPKEPHSRKEILQAEFHLVFTISSEDPANVQVV VQSQECLEKLLDNINMDNYKNYIELCLPSFINVLDSNNANNYRYSPLLSLVLEFITVFLK KKPNDGFLPDEINQYLFEPLAKVLAFSTEDETLQLATEAFSYLIFNTDTRAMEPRLMDIM KVLERLLSLEVSDSAAMNVGPLVVAIFTRFSKEIQPLIGRILEAVVVRLIKTQNISTEQN LLSVLCFLTCNDPKQTVDFLSSFQIDNTDALTLVMRKWIEAFEVIRGEKRIKENIVALSN LFFLNDKRLQKVVVNGNLIPYEGDLIITRSMAKKMPDRYVQVPLYTKIIKLFVSELSFQS KQPNPEQLITSDIKQEVVNANKDDDNDDWEDVDDVLDYDKLKEYIDDDVDEEADDDSDDI TGLMDVKESVVQLLVRFFKEVASKDVSGFHCIYETLSDSERKVLSEALL
Karyopherin Kap114p-mediated trans-repression controls ribosomal gene expression under saline stress. Liao, C.C., Shankar, S., Pi, W.C. et al. EMBO Rep (2020) 21. DOI 10.15252/embr.201948324 · PubMed
Other PDB entries of the same protein (UniProt P53067 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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