Structure of an open and closed conformation of Human Importin Beta bound to the Snurportin1 IBB-domain trapped in the same crystallographic asymmetric unit. Determined by X-ray diffraction at 3.15 Å resolution. Released 2 Jun 2010.
Explore 3LWW in 3D Show helices and sheets RCSB PDB PDBe
3LWW contains 111 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 | 3-8 | 6 | |
| α-helix | 15-31 | 17 | |
| α-helix | 33-45 | 13 | |
| α-helix | 51-63 | 13 | |
| 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 | 170-181 | 12 | |
| α-helix | 188-201 | 14 | |
| α-helix | 206-209 | 4 | |
| α-helix | 212-225 | 14 | |
| α-helix | 231-247 | 17 | |
| α-helix | 250-252 | 3 | |
| α-helix | 256-260 | 5 | |
| α-helix | 261-269 | 9 | |
| α-helix | 273-300 | 28 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-329 | 11 | |
| α-helix | 344-358 | 15 | |
| α-helix | 364-372 | 9 | |
| α-helix | 381-392 | 12 | |
| α-helix | 399-416 | 18 | |
| α-helix | 422-438 | 17 | |
| α-helix | 440-443 | 4 | |
| α-helix | 449-459 | 11 | |
| α-helix | 464-481 | 18 | |
| α-helix | 498-501 | 4 | |
| α-helix | 503-513 | 11 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-537 | 14 | |
| α-helix | 544-561 | 18 | |
| α-helix | 578-592 | 15 | |
| α-helix | 599-613 | 15 | |
| α-helix | 628-635 | 8 | |
| α-helix | 650-657 | 8 | |
| α-helix | 667-677 | 11 | |
| α-helix | 686-688 | 3 | |
| α-helix | 690-696 | 7 | |
| α-helix | 711-715 | 5 | |
| α-helix | 728-730 | 3 | |
| α-helix | 732-744 | 13 | |
| α-helix | 755-758 | 4 | |
| α-helix | 762-775 | 14 | |
| α-helix | 788-790 | 3 | |
| α-helix | 791-806 | 16 | |
| α-helix | 812-828 | 17 | |
| α-helix | 841-843 | 3 | |
| α-helix | 844-851 | 8 | |
| α-helix | 859-869 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-30 | 4 | |
| α-helix | 40-58 | 19 | |
| α-helix | 59-61 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-8 | 6 | |
| α-helix | 9-11 | 3 | |
| α-helix | 15-25 | 11 | |
| α-helix | 33-45 | 13 | |
| α-helix | 51-65 | 15 | |
| α-helix | 70-81 | 12 | |
| α-helix | 85-98 | 14 | |
| α-helix | 109-120 | 12 | |
| α-helix | 121-123 | 3 | |
| α-helix | 130-138 | 9 | |
| α-helix | 144-160 | 17 | |
| α-helix | 170-181 | 12 | |
| α-helix | 188-199 | 12 | |
| α-helix | 202-204 | 3 | |
| α-helix | 206-210 | 5 | |
| α-helix | 212-226 | 15 | |
| α-helix | 231-247 | 17 | |
| α-helix | 249-251 | 3 | |
| α-helix | 256-260 | 5 | |
| α-helix | 261-268 | 8 | |
| α-helix | 273-290 | 18 | |
| α-helix | 298-301 | 4 | |
| α-helix | 305-307 | 3 | |
| α-helix | 314-329 | 16 | |
| α-helix | 344-358 | 15 | |
| α-helix | 364-373 | 10 | |
| α-helix | 380-392 | 13 | |
| α-helix | 399-401 | 3 | |
| α-helix | 403-417 | 15 | |
| α-helix | 422-438 | 17 | |
| α-helix | 449-453 | 5 | |
| α-helix | 454-456 | 3 | |
| α-helix | 469-483 | 15 | |
| α-helix | 499-502 | 4 | |
| α-helix | 504-506 | 3 | |
| α-helix | 528-533 | 6 | |
| α-helix | 548-561 | 14 | |
| α-helix | 580-584 | 5 | |
| α-helix | 600-618 | 19 | |
| α-helix | 626-639 | 14 | |
| α-helix | 640-643 | 4 | |
| α-helix | 644-659 | 16 | |
| α-helix | 664-681 | 18 | |
| α-helix | 686-688 | 3 | |
| α-helix | 689-700 | 12 | |
| α-helix | 709-724 | 16 | |
| α-helix | 725-730 | 6 | |
| α-helix | 732-744 | 13 | |
| α-helix | 755-777 | 23 | |
| α-helix | 787-789 | 3 | |
| α-helix | 791-793 | 3 | |
| α-helix | 794-805 | 12 | |
| α-helix | 812-829 | 18 | |
| α-helix | 832-839 | 8 | |
| α-helix | 841-850 | 10 | |
| α-helix | 859-870 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 40-63 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-1 | A, C | protein | 876 | Homo sapiens | Q14974 (AlphaFold model) |
| Snurportin-1 | B, D | protein | 40 | O95149 (AlphaFold model) |
>3LWW_1 Importin subunit beta-1 (chains A, C) MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAE IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP SVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSA KDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDA LQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKN YAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQ ENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEAR PMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
>3LWW_2 Snurportin-1 (chains B, D) HPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDYVNHARR
Conformational selection in the recognition of the snurportin importin beta binding domain by importin beta. Bhardwaj, A., Cingolani, G. Biochemistry (2010) 49:5042-5047. DOI 10.1021/bi100292y · PubMed
Other PDB entries of the same protein (UniProt Q14974 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3LWW 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.