Crystal structure of mouse Importin alpha in complex with Hendra virus matrix protein minor site NLS2. Determined by X-ray diffraction at 2.1 Å resolution. Released 25 Jan 2023.
Explore 8FUC in 3D Show helices and sheets RCSB PDB PDBe
8FUC 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 | 121-127 | 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 | 223-237 | 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 | 349-363 | 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 | 434-452 | 19 | |
| α-helix | 457-466 | 10 | |
| α-helix | 469-476 | 8 | |
| α-helix | 482-495 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Matrix protein | A | protein | 18 | Hendra virus horse/Australia/Hendra/1994 | O89341 (AlphaFold model) |
| Importin subunit alpha-1 | B | protein | 510 | Mus musculus | P52293 (AlphaFold model) |
| Contaminant peptide KKLARE | F | protein | 6 | Escherichia coli BL21(DE3) |
>8FUC_1 Matrix protein (chains A) VRRAGKYYSVEYCKRKID
>8FUC_2 Importin subunit alpha-1 (chains B) MHHHHHHSSGLVPRGSGMLETAAALFERNHMDSPDLGTDDDDLAMADIGSNQGTVNWSVE DIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFE SAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSAFRDL VIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRL LHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGN IVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLV PFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLLSAKDTKIIQV ILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQRHENESVYKASLNLIEKYFSVE EEEDQNVVPETTSEGFAFQVQDGAPGTFNF
>8FUC_3 Contaminant peptide KKLARE (chains F) KKLARE
Henipavirus Matrix Protein Employs a Non-Classical Nuclear Localization Signal Binding Mechanism. Donnelly, C.M., Vogel, O.A., Edwards, M.R. et al. Viruses (2023) 15. DOI 10.3390/v15061302 · PubMed
Other PDB entries of the same protein (UniProt O89341 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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