SOX2 bound to Importin-alpha 3. Determined by X-ray diffraction at 2.3 Å resolution. Released 28 Oct 2020.
Explore 6WX8 in 3D Show helices and sheets RCSB PDB PDBe
6WX8 contains 75 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 | 85-100 | 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 | 189-198 | 10 | |
| α-helix | 201-206 | 6 | |
| α-helix | 214-227 | 14 | |
| 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 | 316-324 | 9 | |
| α-helix | 327-330 | 4 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-354 | 15 | |
| α-helix | 358-366 | 9 | |
| α-helix | 370-377 | 8 | |
| 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 | 458-464 | 7 | |
| α-helix | 465-467 | 3 | |
| α-helix | 471-484 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 47-62 | 16 | |
| α-helix | 68-79 | 12 | |
| α-helix | 84-103 | 20 | |
| α-helix | 108-110 | 3 | |
| α-helix | 112-113 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 71-80 | 10 | |
| α-helix | 85-100 | 16 | |
| α-helix | 107-112 | 6 | |
| α-helix | 116-123 | 8 | |
| α-helix | 129-143 | 15 | |
| α-helix | 147-155 | 9 | |
| α-helix | 159-165 | 7 | |
| α-helix | 171-185 | 15 | |
| α-helix | 189-198 | 10 | |
| α-helix | 201-206 | 6 | |
| α-helix | 214-227 | 14 | |
| 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 | 316-324 | 9 | |
| 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 | 413-418 | 6 | |
| α-helix | 419-421 | 3 | |
| 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 | 47-62 | 16 | |
| α-helix | 68-79 | 12 | |
| α-helix | 84-103 | 20 | |
| α-helix | 111-113 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha-3 | A, C | protein | 459 | Homo sapiens | O00629 (AlphaFold model) |
| Transcription factor SOX-2 | B, D | protein | 90 | Homo sapiens | P48431 (AlphaFold model) |
>6WX8_1 Importin subunit alpha-3 (chains A, C) SGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHC LERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALG NIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQE ILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQT AALRAVGNIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQVQ AVIDANLVPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLLTV KDAQVVQVVLDGLSNILKMAEDEAETIGNLIEECGGLEKIEQLQNHENEDIYKLAYEIID QFFSSDDIDEDPSLVPEAIQGGTFGFNSSANVPTEGFQF
>6WX8_2 Transcription factor SOX-2 (chains B, D) SDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRL RALHMKEHPDYKYRPRRKTKTLMKKDKYTL
Structural basis for nuclear import selectivity of pioneer transcription factor SOX2. Jagga, B., Edwards, M., Pagin, M. et al. Nat Commun (2021) 12:28-28. DOI 10.1038/s41467-020-20194-0 · 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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