Human importin alpha 3 in complex with Bimax2 peptide. Determined by X-ray diffraction at 3.0 Å resolution. Released 8 Feb 2023.
Explore 8FZM in 3D Show helices and sheets RCSB PDB PDBe
8FZM 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 | 73-80 | 8 | |
| α-helix | 85-99 | 15 | |
| α-helix | 107-112 | 6 | |
| α-helix | 115-122 | 8 | |
| α-helix | 129-142 | 14 | |
| α-helix | 147-155 | 9 | |
| α-helix | 158-165 | 8 | |
| α-helix | 171-186 | 16 | |
| 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 | 332-335 | 4 | |
| α-helix | 340-354 | 15 | |
| α-helix | 358-366 | 9 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-397 | 16 | |
| 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 | 458-465 | 8 | |
| α-helix | 471-482 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-19 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 73-80 | 8 | |
| α-helix | 85-99 | 15 | |
| α-helix | 107-112 | 6 | |
| α-helix | 115-122 | 8 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-155 | 9 | |
| α-helix | 158-165 | 8 | |
| α-helix | 171-186 | 16 | |
| 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 | 256-269 | 14 | |
| 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 | 332-335 | 4 | |
| α-helix | 340-353 | 14 | |
| α-helix | 358-366 | 9 | |
| α-helix | 370-379 | 10 | |
| α-helix | 382-397 | 16 | |
| 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 | 458-465 | 8 | |
| α-helix | 471-482 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-3 | A, C | protein | 459 | Homo sapiens | O00629 (AlphaFold model) |
| Bimax2 | B, D | protein | 27 | synthetic construct |
>8FZM_1 Importin subunit alpha-3 (chains A, C) SGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHC LERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALG NIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQE ILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQT AALRAVGNIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQVQ AVIDANLVPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLLTV KDAQVVQVVLDGLSNILKMAEDEAETIGNLIEECGGLEKIEQLQNHENEDIYKLAYEIID QFFSSDDIDEDPSLVPEAIQGGTFGFNSSANVPTEGFQF
>8FZM_2 Bimax2 (chains B, D) SRRRRRRKRKREWDDDDDPPKKRRRLD
Human importin alpha 3 in complex with Bimax2 peptide. Donnelly, C.M., Forwood, J.K. To be published.
Other PDB entries of the same protein (UniProt O00629 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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