hnRNPK NLS in complex with Importin alpha 1 (KPNA2). Determined by X-ray diffraction at 2.8 Å resolution. Released 17 Nov 2021.
Explore 7CRU in 3D Show helices and sheets RCSB PDB PDBe
7CRU contains 68 α-helices and 0 β-strands across 4 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 | 90-106 | 17 | |
| α-helix | 112-117 | 6 | |
| α-helix | 121-127 | 7 | |
| α-helix | 134-147 | 14 | |
| 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 | 223-236 | 14 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-259 | 14 | |
| α-helix | 265-279 | 15 | |
| α-helix | 283-291 | 9 | |
| α-helix | 295-301 | 7 | |
| α-helix | 307-320 | 14 | |
| α-helix | 325-333 | 9 | |
| α-helix | 336-338 | 3 | |
| α-helix | 340-344 | 5 | |
| 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 | 470-474 | 5 | |
| α-helix | 475-478 | 4 | |
| α-helix | 482-495 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-32 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heterogeneous nuclear ribonucleoprotein K | B, D | protein | 23 | Homo sapiens | P61978 (AlphaFold model) |
| Importin subunit alpha-1 | A, C | protein | 457 | Homo sapiens | P52292 (AlphaFold model) |
>7CRU_1 Heterogeneous nuclear ribonucleoprotein K (chains B, D) WMEFGKRPAEDMEEEQAFKRSRN
>7CRU_2 Importin subunit alpha-1 (chains A, C) TVNWSVDDIVKGINSSNVENQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGRTD CSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGD GSVFRDLVIKYGAVDPLLALLAVPDMSSLACGYLRNLTWTLSNLCRNKNPAPPIDAVEQI LPTLVRLLHHDDPEVLADTCWAISYLTDGPNERIGMVVKTGVVPQLVKLLGASELPIVTP ALRAIGNIVTGTDEQTQVVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQ VVNHGLVPFLVSVLSKADFKTQKEAVWAVTNYTSGGTVEQIVYLVHCGIIEPLMNLLTAK DTKIILVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQNHENESVYKASLSLI EKYFSVEEEEDQNVVPETTSEGYTFQVQDGAPGTFNF
Nuclear import receptors and hnRNPK mediates nuclear import and stress granule localization of SIRLOIN. Yao, J., Tu, Y., Shen, C. et al. Cell Mol Life Sci (2021) 78:7617-7633. DOI 10.1007/s00018-021-03992-7 · PubMed
Other PDB entries of the same protein (UniProt P61978 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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