Structure of importin a5 bound to the N-terminus of Nup50. Determined by X-ray diffraction at 2.7 Å resolution. Released 30 Nov 2011.
Explore 3TJ3 in 3D Show helices and sheets RCSB PDB PDBe
3TJ3 contains 73 α-helices and 6 β-strands across 4 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 | 85-92 | 8 | |
| α-helix | 96-110 | 15 | |
| α-helix | 118-123 | 6 | |
| α-helix | 127-134 | 8 | |
| α-helix | 141-155 | 15 | |
| α-helix | 159-167 | 9 | |
| α-helix | 170-177 | 8 | |
| α-helix | 183-197 | 15 | |
| α-helix | 201-209 | 9 | |
| α-helix | 213-220 | 8 | |
| α-helix | 226-240 | 15 | |
| α-helix | 246-248 | 3 | |
| α-helix | 249-252 | 4 | |
| α-helix | 253-255 | 3 | |
| α-helix | 256-262 | 7 | |
| α-helix | 268-281 | 14 | |
| α-helix | 286-294 | 9 | |
| α-helix | 298-304 | 7 | |
| α-helix | 310-323 | 14 | |
| α-helix | 328-335 | 8 | |
| α-helix | 339-346 | 8 | |
| α-helix | 352-365 | 14 | |
| α-helix | 370-378 | 9 | |
| α-helix | 382-388 | 7 | |
| α-helix | 394-410 | 17 | |
| α-helix | 413-421 | 9 | |
| α-helix | 425-429 | 5 | |
| α-helix | 437-459 | 23 | |
| α-helix | 468-473 | 6 | |
| α-helix | 477-483 | 7 | |
| α-helix | 484-486 | 3 | |
| β-strand | 487 | 1 | 1 |
| α-helix | 490-503 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 85-92 | 8 | |
| α-helix | 96-110 | 15 | |
| α-helix | 118-123 | 6 | |
| α-helix | 127-134 | 8 | |
| α-helix | 141-155 | 15 | |
| α-helix | 159-168 | 10 | |
| α-helix | 170-177 | 8 | |
| α-helix | 183-197 | 15 | |
| α-helix | 201-209 | 9 | |
| α-helix | 213-220 | 8 | |
| α-helix | 226-240 | 15 | |
| α-helix | 246-248 | 3 | |
| α-helix | 249-252 | 4 | |
| α-helix | 253-255 | 3 | |
| α-helix | 256-262 | 7 | |
| α-helix | 268-281 | 14 | |
| α-helix | 286-294 | 9 | |
| α-helix | 298-304 | 7 | |
| α-helix | 310-323 | 14 | |
| α-helix | 328-335 | 8 | |
| α-helix | 339-346 | 8 | |
| α-helix | 352-365 | 14 | |
| α-helix | 370-378 | 9 | |
| α-helix | 382-388 | 7 | |
| α-helix | 394-410 | 17 | |
| α-helix | 413-421 | 9 | |
| α-helix | 425-429 | 5 | |
| α-helix | 437-459 | 23 | |
| α-helix | 467-473 | 7 | |
| α-helix | 477-483 | 7 | |
| α-helix | 484-486 | 3 | |
| β-strand | 487 | 1 | 2 |
| α-helix | 490-503 | 14 | |
| β-strand | 506 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-28 | 2 | |
| β-strand | 29 | 1 | 1 |
| α-helix | 30-31 | 2 | |
| α-helix | 32-37 | 6 | |
| α-helix | 39-40 | 2 | |
| α-helix | 43-45 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-28 | 2 | |
| β-strand | 29 | 1 | 2 |
| α-helix | 30-31 | 2 | |
| α-helix | 32-37 | 6 | |
| α-helix | 39-40 | 2 | |
| β-strand | 43 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-1 | A, B | protein | 447 | Homo sapiens | P52294 (AlphaFold model) |
| Nuclear pore complex protein Nup50 | C, D | protein | 114 | Homo sapiens | Q9UKX7 (AlphaFold model) |
>3TJ3_1 Importin subunit alpha-1 (chains A, B) GFHEAQISNMEMAPGGVITSDMIEMIFSKSPEQQLSATQKFRKLLSKEPNPPIDEVISTP GVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIFIELLSSEFEDV QEQAVWALGNIAGDSTMCRDYVLDCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSP PPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELL MHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNI TAGNRAQIQTVIDANIFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCI KPLCDLLTVMDSKIVQVALNGLENILRLGEQEAKRNGTGINPYCALIEEAYGLDKIEFLQ SHENQEIYQKAFDLIEHYFGTEDEDSS
>3TJ3_2 Nuclear pore complex protein Nup50 (chains C, D) GPLGSMAKRNAEKELTDRNWDQEDEAEEVGTFSMASEEVLKNRAIKKAKRRNVGFESDTG GAFKGFKGLVVPSGGGRFSGFGSGAGGKPLEGLSNGNNITSAPPFASAKAAADP
Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin alpha 5. Pumroy, R.A., Nardozzi, J.D., Hart, D.J. et al. J Biol Chem (2012) 287:2022-2031. DOI 10.1074/jbc.M111.315838 · PubMed
Other PDB entries of the same protein (UniProt P52294 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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