The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution. Determined by X-ray diffraction at 2.53 Å resolution. Released 29 May 2013.
Explore 4E4V in 3D Show helices and sheets RCSB PDB PDBe
4E4V 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 | 78-85 | 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 | 206-211 | 6 | |
| α-helix | 218-220 | 3 | |
| α-helix | 223-236 | 14 | |
| 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 | 340-344 | 5 | |
| α-helix | 349-363 | 15 | |
| α-helix | 367-375 | 9 | |
| α-helix | 379-388 | 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 | 469-474 | 6 | |
| α-helix | 482-495 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 78-85 | 8 | |
| α-helix | 90-105 | 16 | |
| 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 | 176-191 | 16 | |
| α-helix | 194-202 | 9 | |
| α-helix | 206-211 | 6 | |
| 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 | 283-291 | 9 | |
| 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 | 379-388 | 10 | |
| 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 | 469-474 | 6 | |
| α-helix | 475-477 | 3 | |
| α-helix | 482-495 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-2 | A, B | protein | 485 | Homo sapiens | P52292 (AlphaFold model) |
>4E4V_1 Importin subunit alpha-2 (chains A, B) MGSSHHHHHSSGENLYFQGHMLDALNQGTVNWSVDDIVKGINSSNVENQLQATQAARKLL SREKQPPIDNIIRAGLIPKFVSFLGRTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAI PAFISLLASPHAHISEQAVWALGNIAGDGSVFRDLVIKYGAVDPLLALLAVPDMSSLACG YLRNLTWTLSNLCRNKNPAPPIDAVEQILPTLVRLLHHDDPEVLADTCWAISYLTDGPNE RIGMVVKTGVVPQLVKLLGASELPIVTPALRAIGNIVTGTDEQTQVVIDAGALAVFPSLL TNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLVPFLVSVLSKADFKTQKEAVWAVTNY TSGGTVEQIVYLVHCGIIEPLMNLLTAKDTKIILVILDAISNIFQAAEKLGETEKLSIMI EECGGLDKIEALQNHENESVYRASLSLIEKYFSVEEEEDQNVVPETTSEGYTFQVQDGAP GTFNF
| ID | Name | Formula | Copies |
|---|---|---|---|
| DTT | 2,3-dihydroxy-1,4-dithiobutane | C4 H10 O2 S2 | 2 |
Water and common crystallization additives (GOL) are not listed.
The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution. Hang, P.C., Miknis, Z.J., Franke, W.A. et al. 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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