Importin Beta aa1-442 bound to five FxFG repeats from yeast Nsp1p. Second crystal form. Determined by X-ray diffraction at 2.8 Å resolution. Released 17 Oct 2003.
Explore 1O6O in 3D Show helices and sheets RCSB PDB PDBe
1O6O contains 88 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 | 3-9 | 7 | |
| α-helix | 15-31 | 17 | |
| α-helix | 33-45 | 13 | |
| α-helix | 51-62 | 12 | |
| α-helix | 70-81 | 12 | |
| α-helix | 85-98 | 14 | |
| α-helix | 108-120 | 13 | |
| α-helix | 121-123 | 3 | |
| α-helix | 129-138 | 10 | |
| α-helix | 144-160 | 17 | |
| α-helix | 163-166 | 4 | |
| α-helix | 170-181 | 12 | |
| α-helix | 188-201 | 14 | |
| α-helix | 202-204 | 3 | |
| α-helix | 206-210 | 5 | |
| α-helix | 212-225 | 14 | |
| α-helix | 231-247 | 17 | |
| α-helix | 250-252 | 3 | |
| α-helix | 253-255 | 3 | |
| α-helix | 256-260 | 5 | |
| α-helix | 261-269 | 9 | |
| α-helix | 273-301 | 29 | |
| α-helix | 314-329 | 16 | |
| α-helix | 344-358 | 15 | |
| α-helix | 360-375 | 16 | |
| α-helix | 380-392 | 13 | |
| α-helix | 399-407 | 9 | |
| α-helix | 410-418 | 9 | |
| α-helix | 422-438 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-9 | 7 | |
| α-helix | 15-31 | 17 | |
| α-helix | 33-45 | 13 | |
| α-helix | 51-62 | 12 | |
| α-helix | 70-81 | 12 | |
| α-helix | 85-98 | 14 | |
| α-helix | 108-120 | 13 | |
| α-helix | 121-123 | 3 | |
| α-helix | 129-138 | 10 | |
| α-helix | 144-160 | 17 | |
| α-helix | 163-166 | 4 | |
| α-helix | 171-181 | 11 | |
| α-helix | 188-201 | 14 | |
| α-helix | 202-204 | 3 | |
| α-helix | 206-210 | 5 | |
| α-helix | 212-225 | 14 | |
| α-helix | 231-247 | 17 | |
| α-helix | 250-252 | 3 | |
| α-helix | 253-255 | 3 | |
| α-helix | 256-260 | 5 | |
| α-helix | 261-269 | 9 | |
| α-helix | 273-301 | 29 | |
| α-helix | 314-329 | 16 | |
| α-helix | 344-358 | 15 | |
| α-helix | 360-375 | 16 | |
| α-helix | 380-392 | 13 | |
| α-helix | 399-407 | 9 | |
| α-helix | 410-418 | 9 | |
| α-helix | 422-435 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-12 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin beta-1 subunit | A, B, C | protein | 442 | HOMO SAPIENS | Q14974 (AlphaFold model) |
| Nucleoporin NSP1 | D, E, F | protein | 119 | SACCHAROMYCES CEREVISIAE | P14907 (AlphaFold model) |
>1O6O_1 IMPORTIN BETA-1 SUBUNIT (chains A, B, C) MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLHTLGTETYRPSSASQCVAGIACAE IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP SVVVRDTAAWTVGRICELLPEA
>1O6O_2 NUCLEOPORIN NSP1 (chains D, E, F) MGSSTKSNEKKDSGSSKPAFSFGAKPDEKKNDEVSKPAFSFGAKANEKKESDESKSAFSF GSKPTGKEEGDGAKAAISFGAKPEEQKSSDTSKPAFTFGAQKDNEKKTEESSTGKSMQA
Glfg and Fxfg Nucleoporins Bind to Overlapping Sites on Importin-Beta. Bayliss, R., Littlewood, T., Strawn, L.A. et al. J Biol Chem (2002) 277:50597. DOI 10.1074/JBC.M209037200 · PubMed
Other PDB entries of the same protein (UniProt Q14974 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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