Structure of importin a3 bound to the p50- and p65-NLSs. Determined by X-ray diffraction at 2.85 Å resolution. Released 19 Jan 2022.
Explore 7LF4 in 3D Show helices and sheets RCSB PDB PDBe
7LF4 contains 66 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 | 76-79 | 4 | |
| α-helix | 85-100 | 16 | |
| α-helix | 107-112 | 6 | |
| α-helix | 116-122 | 7 | |
| α-helix | 129-142 | 14 | |
| α-helix | 147-155 | 9 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-185 | 15 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-206 | 6 | |
| α-helix | 214-227 | 14 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-272 | 17 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 316-324 | 9 | |
| α-helix | 327-330 | 4 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-354 | 15 | |
| α-helix | 358-366 | 9 | |
| α-helix | 369-379 | 11 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-409 | 9 | |
| α-helix | 413-418 | 6 | |
| α-helix | 419-421 | 3 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-465 | 8 | |
| α-helix | 471-484 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 439-442 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 79-81 | 3 | |
| α-helix | 85-100 | 16 | |
| α-helix | 107-112 | 6 | |
| α-helix | 115-122 | 8 | |
| α-helix | 129-142 | 14 | |
| α-helix | 147-155 | 9 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-185 | 15 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-206 | 6 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-271 | 16 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 316-324 | 9 | |
| α-helix | 328-330 | 3 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-354 | 15 | |
| α-helix | 358-366 | 9 | |
| α-helix | 369-379 | 11 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-409 | 9 | |
| α-helix | 413-418 | 6 | |
| α-helix | 419-421 | 3 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-465 | 8 | |
| α-helix | 471-484 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-3 | A, C | protein | 521 | Homo sapiens | O00629 (AlphaFold model) |
| Nuclear factor NF-kappa-B p105 subunit | B, F | protein | 14 | Homo sapiens | P19838 (AlphaFold model) |
| Transcription factor p65 | D, E | protein | 22 | Homo sapiens | Q04206 (AlphaFold model) |
>7LF4_1 Importin subunit alpha-3 (chains A, C) MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPHEDICEDS DIDGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILV HCLERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWA LGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETI QEILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKV QTAALRAVGNIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQ VQAVIDANLVPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLL TVKDAQVVQVVLDGLSNILKMAEDEAETIGNLIEECGGLEKIEQLQNHENEDIYKLAYEI IDQFFSSDDIDEDPSLVPEAIQGGTFGFNSSANVPTEGFQF
>7LF4_2 Nuclear factor NF-kappa-B p105 subunit (chains B, F) DKEEVQRKRQKLMP
>7LF4_3 Transcription factor p65 (chains D, E) DRHRIEEKRKRTYETFKSIMKK
Differential recognition of canonical NF-kappa B dimers by Importin alpha 3. Florio, T.J., Lokareddy, R.K., Yeggoni, D.P. et al. Nat Commun (2022) 13:1207-1207. DOI 10.1038/s41467-022-28846-z · PubMed
Other PDB entries of the same protein (UniProt O00629 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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