The cryo-EM structure of nuclear transport receptor Kap114p complex with yeast TATA-box binding protein. Determined by electron microscopy at 4.03 Å resolution. Released 20 Sept 2023.
Explore 8H5B in 3D Show helices and sheets RCSB PDB PDBe
8H5B contains 58 α-helices and 14 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 | 5-10 | 6 | |
| α-helix | 17-30 | 14 | |
| α-helix | 33-45 | 13 | |
| α-helix | 51-64 | 14 | |
| α-helix | 65-69 | 5 | |
| α-helix | 84-99 | 16 | |
| α-helix | 105-126 | 22 | |
| α-helix | 130-135 | 6 | |
| α-helix | 136-141 | 6 | |
| α-helix | 144-157 | 14 | |
| α-helix | 160-164 | 5 | |
| α-helix | 168-181 | 14 | |
| α-helix | 187-206 | 20 | |
| α-helix | 213-235 | 23 | |
| α-helix | 244-263 | 20 | |
| α-helix | 266-268 | 3 | |
| α-helix | 271-290 | 20 | |
| α-helix | 303-320 | 18 | |
| α-helix | 328-341 | 14 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-354 | 9 | |
| α-helix | 356-363 | 8 | |
| α-helix | 372-381 | 10 | |
| α-helix | 385-402 | 18 | |
| α-helix | 406-421 | 16 | |
| α-helix | 429-447 | 19 | |
| α-helix | 453-469 | 17 | |
| α-helix | 477-493 | 17 | |
| α-helix | 499-514 | 16 | |
| α-helix | 517-520 | 4 | |
| α-helix | 523-541 | 19 | |
| α-helix | 549-560 | 12 | |
| α-helix | 571-587 | 17 | |
| α-helix | 592-605 | 14 | |
| α-helix | 611-633 | 23 | |
| α-helix | 641-655 | 15 | |
| β-strand | 663 | 1 | 1 |
| α-helix | 665-681 | 17 | |
| α-helix | 685-701 | 17 | |
| β-strand | 702 | 1 | 1 |
| α-helix | 704-706 | 3 | |
| α-helix | 708-721 | 14 | |
| α-helix | 728-731 | 4 | |
| α-helix | 734-744 | 11 | |
| α-helix | 749-766 | 18 | |
| α-helix | 770-786 | 17 | |
| α-helix | 788-797 | 10 | |
| β-strand | 799 | 1 | 2 |
| β-strand | 804 | 1 | 2 |
| α-helix | 805-819 | 15 | |
| α-helix | 823-837 | 15 | |
| α-helix | 842-845 | 4 | |
| α-helix | 879-895 | 17 | |
| α-helix | 935-940 | 6 | |
| α-helix | 965-977 | 13 | |
| α-helix | 984-989 | 6 | |
| α-helix | 996-999 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 64-65 | 2 | |
| β-strand | 66-75 | 10 | 3 |
| α-helix | 82-88 | 7 | |
| β-strand | 93 | 1 | 3 |
| β-strand | 102-105 | 4 | 3 |
| β-strand | 112-115 | 4 | 3 |
| β-strand | 120-124 | 5 | 3 |
| α-helix | 129-145 | 17 | |
| β-strand | 156-165 | 10 | 3 |
| α-helix | 172-179 | 8 | |
| β-strand | 184 | 1 | 3 |
| β-strand | 194-197 | 4 | 3 |
| β-strand | 202-206 | 5 | 3 |
| β-strand | 211-215 | 5 | 3 |
| α-helix | 220-234 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-5 | A | protein | 1004 | Saccharomyces cerevisiae S288C | P53067 (AlphaFold model) |
| TATA-box-binding protein | B | protein | 180 | Saccharomyces cerevisiae S288C | P13393 (AlphaFold model) |
>8H5B_1 Importin subunit beta-5 (chains A) MDINELIIGAQSADKHTREVAETQLLQWCDSDASQVFKALANVALQHEASLESRQFALLS LRKLITMYWSPGFESYRSTSNVEIDVKDFIREVLLKLCLNDNENTKIKNGASYCIVQISA VDFPDQWPQLLTVIYDAISHQHSLNAMSLLNEIYDDVVSEEMFFEGGIGLATMEIVFKVL NTETSTLIAKIAALKLLKACLLQMSSHNEYDEASRKSFVSQCLATSLQILGQLLTLNFGN VDVISQLKFKSIIYENLVFIKNDFSRKHFSSELQKQFKIMAIQDLENVTHINANVETTES EPLLETVHDCSIYIVEFLTSVCTLQFSVEEMNKIITSLTILCQLSSETREIWTSDFNTFV SKETGLAASYNVRDQANEFFTSLPNPQLSLIFKVVSNDIEHSTCNYSTLESLLYLLQCIL LNDDEITGENIDQSLQILIKTLENILVSQEIPELILARAILTIPRVLDKFIDALPDIKPL TSAFLAKSLNLALKSDKELIKSATLIAFTYYCYFAELDSVLGPEVCSETQEKVIRIINQV SSDAEEDTNGALMEVLSQVISYNPKEPHSRKEILQAEFHLVFTISSEDPANVQVVVQSQE CLEKLLDNINMDNYKNYIELCLPSFINVLDSNNANNYRYSPLLSLVLEFITVFLKKKPND GFLPDEINQYLFEPLAKVLAFSTEDETLQLATEAFSYLIFNTDTRAMEPRLMDIMKVLER LLSLEVSDSAAMNVGPLVVAIFTRFSKEIQPLIGRILEAVVVRLIKTQNISTEQNLLSVL CFLTCNDPKQTVDFLSSFQIDNTDALTLVMRKWIEAFEVIRGEKRIKENIVALSNLFFLN DKRLQKVVVNGNLIPYEGDLIITRSMAKKMPDRYVQVPLYTKIIKLFVSELSFQSKQPNP EQLITSDIKQEVVNANKDDDNDDWEDVDDVLDYDKLKEYIDDDVDEEADDDSDDITGLMD VKESVVQLLVRFFKEVASKDVSGFHCIYETLSDSERKVLSEALL
>8H5B_2 TATA-box-binding protein (chains B) SGIVPTLQNIVATVTLGCRLDLKTVALHARNAEYNPKRFAAVIMRIREPKTTALIFASGK MVVTGAKSEDDSKLASRKYARIIQKIGFAAKFTDFKIQNIVGSCDVKFPIRLEGLAFSHG TFSSYEPELFPGLIYRMVKPKIVLLIFVSGKIVLTGAKQREEIYQAFEAIYPVLSEFRKM
Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding protein. Liao, C.C., Wang, Y.S., Pi, W.C. et al. Nat Commun (2023) 14:5518-5518. DOI 10.1038/s41467-023-41206-9 · 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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