Crystal structure of importin-alpha3 bound to the 53BP1 nuclear localization signal. Determined by X-ray diffraction at 1.9 Å resolution. Released 21 Dec 2022.
Explore 8HKW in 3D Show helices and sheets RCSB PDB PDBe
8HKW contains 72 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 | 72-79 | 8 | |
| α-helix | 85-100 | 16 | |
| α-helix | 107-113 | 7 | |
| α-helix | 116-122 | 7 | |
| α-helix | 129-142 | 14 | |
| α-helix | 147-155 | 9 | |
| α-helix | 158-165 | 8 | |
| α-helix | 171-185 | 15 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-205 | 5 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-270 | 15 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-311 | 14 | |
| α-helix | 316-323 | 8 | |
| α-helix | 327-330 | 4 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-354 | 15 | |
| α-helix | 358-366 | 9 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-409 | 9 | |
| α-helix | 413-417 | 5 | |
| α-helix | 418-421 | 4 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-464 | 7 | |
| α-helix | 465-467 | 3 | |
| α-helix | 471-484 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 72-79 | 8 | |
| α-helix | 85-100 | 16 | |
| α-helix | 107-112 | 6 | |
| α-helix | 116-122 | 7 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-155 | 9 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-185 | 15 | |
| α-helix | 189-197 | 9 | |
| α-helix | 201-205 | 5 | |
| α-helix | 214-228 | 15 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-250 | 14 | |
| α-helix | 256-270 | 15 | |
| α-helix | 274-282 | 9 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-294 | 5 | |
| α-helix | 298-311 | 14 | |
| α-helix | 316-323 | 8 | |
| α-helix | 327-330 | 4 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-354 | 15 | |
| α-helix | 358-366 | 9 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-398 | 17 | |
| α-helix | 401-409 | 9 | |
| α-helix | 413-417 | 5 | |
| α-helix | 418-421 | 4 | |
| α-helix | 425-441 | 17 | |
| α-helix | 446-455 | 10 | |
| α-helix | 458-464 | 7 | |
| α-helix | 465-467 | 3 | |
| α-helix | 471-484 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1669-1672 | 4 | |
| α-helix | 1673-1677 | 5 | |
| α-helix | 1683-1685 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-3 | A, B | protein | 416 | Homo sapiens | O00629 (AlphaFold model) |
| Peptide from TP53-binding protein 1 | C, D | protein | 22 | Homo sapiens | Q12888 (AlphaFold model) |
>8HKW_1 Importin subunit alpha-3 (chains A, B) NTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHCLERDDNP SLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALGNIIGDGP QCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQEILPALCV LIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQTAALRAVG NIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQVQAVIDANL VPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLLTVKDAQVVQ VVLDGLSNILKMAEDEAETIGNLIEECGGLEKIEQLQNHENEDIYKLAYEIIDQFF
>8HKW_2 Peptide from TP53-binding protein 1 (chains C, D) SGKRKLITSEEERSPAKRGRKS
Crystallographic data of an importin-alpha 3 dimer in which the two protomers are bridged by a bipartite nuclear localization signal. Matsuura, Y. Data Brief (2023) 47:108988-108988. DOI 10.1016/j.dib.2023.108988 · 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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