Importin alpha 2 in complex with ATF2 basic region. Determined by X-ray diffraction at 2.2 Å resolution. Released 17 Sept 2025.
Explore 9Y0R in 3D Show helices and sheets RCSB PDB PDBe
9Y0R contains 32 α-helices and 0 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 | 78-86 | 9 | |
| α-helix | 90-104 | 15 | |
| α-helix | 112-117 | 6 | |
| α-helix | 121-128 | 8 | |
| α-helix | 134-148 | 15 | |
| α-helix | 152-160 | 9 | |
| α-helix | 163-170 | 8 | |
| α-helix | 176-192 | 17 | |
| α-helix | 194-202 | 9 | |
| α-helix | 206-212 | 7 | |
| α-helix | 218-220 | 3 | |
| α-helix | 223-236 | 14 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-260 | 15 | |
| α-helix | 265-278 | 14 | |
| α-helix | 283-291 | 9 | |
| α-helix | 295-302 | 8 | |
| α-helix | 307-321 | 15 | |
| α-helix | 325-333 | 9 | |
| α-helix | 336-339 | 4 | |
| α-helix | 340-343 | 4 | |
| α-helix | 349-363 | 15 | |
| α-helix | 367-375 | 9 | |
| α-helix | 379-387 | 9 | |
| α-helix | 391-407 | 17 | |
| α-helix | 410-418 | 9 | |
| α-helix | 422-427 | 6 | |
| α-helix | 428-430 | 3 | |
| α-helix | 434-454 | 21 | |
| α-helix | 457-466 | 10 | |
| α-helix | 469-477 | 9 | |
| α-helix | 482-494 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-1 | A | protein | 510 | Mus musculus | P52293 (AlphaFold model) |
| Cyclic AMP-dependent transcription factor ATF-2 | B | protein | 27 | Homo sapiens | P15336 (AlphaFold model) |
>9Y0R_1 Importin subunit alpha-1 (chains A) MHHHHHHSSGLVPRGSGMLETAAALFERNHMDSPDLGTDDDDLAMADIGSNQGTVNWSVE DIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFE SAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSAFRDL VIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRL LHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGN IVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLV PFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLLSAKDTKIIQV ILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQRHENESVYKASLNLIEKYFSVE EEEDQNVVPETTSEGFAFQVQDGAPGTFNF
>9Y0R_2 Cyclic AMP-dependent transcription factor ATF-2 (chains B) DEKRRKFLERNRAAASRCRQKRKVWVQ
Structural and functional characterisation of ATF2 nuclear import reveals paralogue-selective importin-alpha recognition and a non-canonical NLS formed in trans. Ghafoori, S.M., Pavan, S., Duc, T.X. et al. Life Sci Alliance (2026) 9. DOI 10.26508/lsa.202503543 · PubMed
Other PDB entries of the same protein (UniProt P52293 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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