rImp_alpha_B54NLS. Determined by X-ray diffraction at 2.1 Å resolution. Released 9 Jan 2013.
Explore 2YNS in 3D Show helices and sheets RCSB PDB PDBe
2YNS contains 69 α-helices and 0 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 | 74-81 | 8 | |
| α-helix | 86-100 | 15 | |
| α-helix | 108-113 | 6 | |
| α-helix | 117-123 | 7 | |
| α-helix | 130-143 | 14 | |
| α-helix | 148-156 | 9 | |
| α-helix | 159-165 | 7 | |
| α-helix | 166-168 | 3 | |
| α-helix | 172-186 | 15 | |
| α-helix | 190-198 | 9 | |
| α-helix | 202-207 | 6 | |
| α-helix | 215-229 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-240 | 4 | |
| α-helix | 243-250 | 8 | |
| α-helix | 256-269 | 14 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-291 | 6 | |
| α-helix | 292-294 | 3 | |
| α-helix | 298-311 | 14 | |
| α-helix | 316-323 | 8 | |
| α-helix | 327-336 | 10 | |
| α-helix | 341-354 | 14 | |
| α-helix | 359-367 | 9 | |
| α-helix | 371-380 | 10 | |
| α-helix | 383-399 | 17 | |
| α-helix | 402-410 | 9 | |
| α-helix | 414-419 | 6 | |
| α-helix | 420-422 | 3 | |
| α-helix | 426-449 | 24 | |
| α-helix | 456-463 | 8 | |
| α-helix | 466-472 | 7 | |
| α-helix | 473-475 | 3 | |
| α-helix | 479-492 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 75-81 | 7 | |
| α-helix | 86-100 | 15 | |
| α-helix | 108-113 | 6 | |
| α-helix | 117-122 | 6 | |
| α-helix | 123-125 | 3 | |
| α-helix | 130-144 | 15 | |
| α-helix | 148-156 | 9 | |
| α-helix | 159-165 | 7 | |
| α-helix | 166-168 | 3 | |
| α-helix | 172-186 | 15 | |
| α-helix | 190-198 | 9 | |
| α-helix | 202-207 | 6 | |
| α-helix | 215-229 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-240 | 4 | |
| α-helix | 243-250 | 8 | |
| α-helix | 256-269 | 14 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-291 | 6 | |
| α-helix | 292-294 | 3 | |
| α-helix | 298-311 | 14 | |
| α-helix | 316-323 | 8 | |
| α-helix | 327-336 | 10 | |
| α-helix | 341-354 | 14 | |
| α-helix | 359-367 | 9 | |
| α-helix | 371-380 | 10 | |
| α-helix | 383-399 | 17 | |
| α-helix | 402-410 | 9 | |
| α-helix | 414-419 | 6 | |
| α-helix | 420-422 | 3 | |
| α-helix | 426-449 | 24 | |
| α-helix | 456-463 | 8 | |
| α-helix | 466-472 | 7 | |
| α-helix | 473-475 | 3 | |
| α-helix | 479-492 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-1A | A, B | protein | 490 | ORYZA SATIVA | Q71VM4 (AlphaFold model) |
| B54NLS | C, D | protein | 12 | SYNTHETIC CONSTRUCT |
>2YNS_1 IMPORTIN SUBUNIT ALPHA-1A (chains A, B) GSGMKETAAAKFERQHMDSPDLGTDDDDKAMADIGSSLPAMIGGVYSDDNNLQLEATTQF RKLLSIERSPPIEEVIQSGVVPRFVQFLTREDFPQLQFEAAWALTNIASGTSENTKVVID HGAVPIFVKLLGSSSDDVREQAVWALGNVAGDSPKCRDLVLANGALLPLLAQLNEHTKLS MLRNATWTLSNFCRGKPQPSFEQTRPALPALARLIHSNDEEVLTDACWALSYLSDGTNDK IQAVIEAGVCPRLVELLLHPSPSVLIPALRTVGNIVTGDDAQTQCIIDHQALPCLLSLLT QNLKKSIKKEACWTISNITAGNKDQIQAVINAGIIGPLVNLLQTAEFDIKKEAAWAISNA TSGGSHDQIKYLVSEGCIKPLCDLLICPDIRIVTVCLEGLENILKVGETDKTLAAGDVNV FSQMIDEAEGLEKIENLQSHDNNEIYEKAVKILEAYWMDEEDDTMGATTVAAPQGATFDF GQGGGAAQFK
>2YNS_2 B54NLS (chains C, D) SVLGKRKRHPKV
Crystal Structure of Rice Importin-Alpha and Structural Basis of its Interaction with Plant-Specific Nuclear Localization Signals. Chang, C.-W., Counago, R.L.M., Williams, S.J. et al. Plant Cell (2012) 24:5074. DOI 10.1105/TPC.112.104422 · PubMed
Other PDB entries of the same protein (UniProt Q71VM4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2YNS 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.