Cryo-EM structure of the Importin beta:Histone H1.0 complex. Determined by electron microscopy at 7.5 Å resolution. Released 27 Feb 2019.
Explore 6N89 in 3D Show helices and sheets RCSB PDB PDBe
6N89 contains 53 α-helices and 3 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 | 3-9 | 7 | |
| α-helix | 15-19 | 5 | |
| α-helix | 21-31 | 11 | |
| α-helix | 36-45 | 10 | |
| α-helix | 51-62 | 12 | |
| α-helix | 70-82 | 13 | |
| α-helix | 85-98 | 14 | |
| α-helix | 108-120 | 13 | |
| α-helix | 129-138 | 10 | |
| α-helix | 144-160 | 17 | |
| α-helix | 170-180 | 11 | |
| α-helix | 188-201 | 14 | |
| α-helix | 206-209 | 4 | |
| α-helix | 212-225 | 14 | |
| α-helix | 231-246 | 16 | |
| α-helix | 253-255 | 3 | |
| α-helix | 256-261 | 6 | |
| α-helix | 262-269 | 8 | |
| α-helix | 273-303 | 31 | |
| α-helix | 314-329 | 16 | |
| α-helix | 344-358 | 15 | |
| α-helix | 363-374 | 12 | |
| α-helix | 383-392 | 10 | |
| α-helix | 399-416 | 18 | |
| α-helix | 422-438 | 17 | |
| α-helix | 449-459 | 11 | |
| α-helix | 464-481 | 18 | |
| α-helix | 494 | 1 | |
| α-helix | 500-513 | 14 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-537 | 14 | |
| α-helix | 545-561 | 17 | |
| α-helix | 571-587 | 17 | |
| α-helix | 599-613 | 15 | |
| α-helix | 615-617 | 3 | |
| α-helix | 627-639 | 13 | |
| α-helix | 650-657 | 8 | |
| α-helix | 665-677 | 13 | |
| α-helix | 687-689 | 3 | |
| α-helix | 690-701 | 12 | |
| α-helix | 711-715 | 5 | |
| α-helix | 717-721 | 5 | |
| α-helix | 732-744 | 13 | |
| α-helix | 755-758 | 4 | |
| α-helix | 761-775 | 15 | |
| α-helix | 785-804 | 20 | |
| α-helix | 812-828 | 17 | |
| α-helix | 833-837 | 5 | |
| α-helix | 843-851 | 9 | |
| α-helix | 857-869 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-38 | 11 | |
| β-strand | 46 | 1 | 1 |
| α-helix | 47-55 | 9 | |
| α-helix | 64-77 | 14 | |
| β-strand | 81-87 | 7 | 1 |
| β-strand | 90-95 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-1 | A | protein | 876 | Homo sapiens | Q14974 (AlphaFold model) |
| Histone H1.0 | B | protein | 194 | Homo sapiens | P07305 (AlphaFold model) |
>6N89_1 Importin subunit beta-1 (chains A) MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAE IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP SVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSA KDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDA LQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKN YAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQ ENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEAR PMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
>6N89_2 Histone H1.0 (chains B) MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKV GENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVATP KKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPVK PKAKSSAKRAGKKK
Fuzzy Interactions Form and Shape the Histone Transport Complex. Ivic, N., Potocnjak, M., Solis-Mezarino, V. et al. Mol Cell (2019) 73:1191. DOI 10.1016/j.molcel.2019.01.032 · PubMed
Other PDB entries of the same protein (UniProt Q14974 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6N89 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.