Crystal structure of closed dimer of human importin-alpha1 (Rch1). Determined by X-ray diffraction at 2.63 Å resolution. Released 21 Jan 2015.
Explore 3WPT in 3D Show helices and sheets RCSB PDB PDBe
3WPT contains 64 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 | 78-86 | 9 | |
| α-helix | 90-105 | 16 | |
| α-helix | 112-117 | 6 | |
| α-helix | 121-127 | 7 | |
| α-helix | 134-147 | 14 | |
| α-helix | 152-160 | 9 | |
| α-helix | 163-168 | 6 | |
| α-helix | 176-191 | 16 | |
| α-helix | 194-202 | 9 | |
| α-helix | 206-211 | 6 | |
| α-helix | 218-220 | 3 | |
| α-helix | 223-235 | 13 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-259 | 14 | |
| α-helix | 265-278 | 14 | |
| α-helix | 283-291 | 9 | |
| α-helix | 295-301 | 7 | |
| α-helix | 307-320 | 14 | |
| α-helix | 325-333 | 9 | |
| α-helix | 337-339 | 3 | |
| α-helix | 340-344 | 5 | |
| α-helix | 349-362 | 14 | |
| α-helix | 367-375 | 9 | |
| α-helix | 378-388 | 11 | |
| α-helix | 391-407 | 17 | |
| α-helix | 410-418 | 9 | |
| α-helix | 422-427 | 6 | |
| α-helix | 428-430 | 3 | |
| α-helix | 434-452 | 19 | |
| α-helix | 457-466 | 10 | |
| α-helix | 469-474 | 6 | |
| α-helix | 482-493 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 78-85 | 8 | |
| α-helix | 90-104 | 15 | |
| α-helix | 112-116 | 5 | |
| α-helix | 121-127 | 7 | |
| α-helix | 134-147 | 14 | |
| α-helix | 152-160 | 9 | |
| α-helix | 163-169 | 7 | |
| α-helix | 170-172 | 3 | |
| α-helix | 176-191 | 16 | |
| α-helix | 194-202 | 9 | |
| α-helix | 206-211 | 6 | |
| 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 | 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 | 434-453 | 20 | |
| α-helix | 457-466 | 10 | |
| α-helix | 469-474 | 6 | |
| α-helix | 482-495 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-1 | A, B | protein | 423 | Homo sapiens | P52292 (AlphaFold model) |
>3WPT_1 Importin subunit alpha-1 (chains A, B) NWSVDDIVKGINSSNVENQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGRTDCS PIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGS VFRDLVIKYGAVDPLLALLAVPDMSSLACGYLRNLTWTLSNLCRNKNPAPPIDAVEQILP TLVRLLHHDDPEVLADTCWAISYLTDGPNERIGMVVKTGVVPQLVKLLGASELPIVTPAL RAIGNIVTGTDEQTQVVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVV NHGLVPFLVSVLSKADFKTQKEAVWAVTNYTSGGTVEQIVYLVHCGIIEPLMNLLTAKDT KIILVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQNHENESVYKASLSLIEK YFS
Crystal structure of closed dimer of human importin-alpha1 (Rch1). Miyatake, H. To be published.
Other PDB entries of the same protein (UniProt P52292 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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