Structure of mouse importin a1 bound to Pom121NLS. Determined by X-ray diffraction at 1.81 Å resolution. Released 13 Jan 2016.
Explore 4YI0 in 3D Show helices and sheets RCSB PDB PDBe
4YI0 contains 35 α-helices and 0 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 | 315-317 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 78-85 | 8 | |
| α-helix | 90-104 | 15 | |
| α-helix | 112-117 | 6 | |
| α-helix | 121-127 | 7 | |
| α-helix | 134-148 | 15 | |
| α-helix | 152-160 | 9 | |
| α-helix | 163-170 | 8 | |
| α-helix | 176-190 | 15 | |
| α-helix | 194-202 | 9 | |
| α-helix | 206-212 | 7 | |
| α-helix | 218-220 | 3 | |
| α-helix | 223-237 | 15 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-259 | 14 | |
| α-helix | 265-278 | 14 | |
| α-helix | 283-290 | 8 | |
| α-helix | 295-302 | 8 | |
| α-helix | 307-320 | 14 | |
| α-helix | 325-333 | 9 | |
| α-helix | 336-339 | 4 | |
| α-helix | 340-343 | 4 | |
| α-helix | 349-362 | 14 | |
| α-helix | 367-375 | 9 | |
| α-helix | 378-387 | 10 | |
| α-helix | 391-407 | 17 | |
| α-helix | 410-418 | 9 | |
| α-helix | 422-427 | 6 | |
| α-helix | 428-430 | 3 | |
| α-helix | 434-453 | 20 | |
| α-helix | 457-466 | 10 | |
| α-helix | 469-475 | 7 | |
| α-helix | 476-478 | 3 | |
| α-helix | 482-491 | 10 | |
| α-helix | 492-496 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-1 | C | protein | 460 | Mus musculus | P52293 (AlphaFold model) |
| Nuclear envelope pore membrane protein POM 121 | A | protein | 30 | Rattus norvegicus | P52591 (AlphaFold model) |
>4YI0_1 Importin subunit alpha-1 (chains C) NQGTVNWSVEDIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLG KTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNI AGDGSAFRDLVIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAV EQILPTLVRLLHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPI VTPALRAIGNIVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQ IQQVVNHGLVPFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLL SAKDTKIIQVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQRHENESVYKASL NLIEKYFSVEEEEDQNVVPETTSEGFAFQVQDGAPGTFNF
>4YI0_2 Nuclear envelope pore membrane protein POM 121 (chains A) LKEKKKRTVAEEDQLHLDGQENKRRRHDSS
Mammalian Pom121 and yeast Heh2 share IBB-like NLSs that support targeting to the inner nuclear membrane. Kralt, A., Basheer, N.J., van den Boom, V. et al. To be published.
Other PDB entries of the same protein (UniProt P52293 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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