Crystal structure of mouse importin-alpha1 bound to non-phosphorylated NLS of EBNA1. Determined by X-ray diffraction at 2.2 Å resolution. Released 25 Jan 2017.
Explore 5WUN in 3D Show helices and sheets RCSB PDB PDBe
5WUN contains 33 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 | 78-85 | 8 | |
| 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 | 176-190 | 15 | |
| α-helix | 194-202 | 9 | |
| α-helix | 206-211 | 6 | |
| 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 | 283-290 | 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 | 434-452 | 19 | |
| α-helix | 457-466 | 10 | |
| α-helix | 469-475 | 7 | |
| α-helix | 476-478 | 3 | |
| α-helix | 482-495 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-1 | A | protein | 460 | Mus musculus | P52293 (AlphaFold model) |
| Epstein-Barr nuclear antigen 1 | B, C | protein | 9 | Epstein-Barr virus | P03211 (AlphaFold model) |
>5WUN_1 Importin subunit alpha-1 (chains A) NQGTVNWSVEDIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLG KTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNI AGDGSAFRDLVIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAV EQILPTLVRLLHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPI VTPALRAIGNIVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQ IQQVVNHGLVPFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLL SAKDTKIIQVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQRHENESVYKASL NLIEKYFSVEEEEDQNVVPETTSEGFAFQVQDGAPGTFNF
>5WUN_2 Epstein-Barr nuclear antigen 1 (chains B, C) EKRPRSPSS
Structural basis for the regulation of nuclear import of Epstein-Barr virus nuclear antigen 1 (EBNA1) by phosphorylation of the nuclear localization signal. Nakada, R., Hirano, H., Matsuura, Y. Biochem Biophys Res Commun (2017) 484:113-117. DOI 10.1016/j.bbrc.2017.01.063 · 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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