The crystal structure of phosphorylated IRF-3. Determined by X-ray diffraction at 1.8 Å resolution. Released 4 Aug 2010.
Explore 3A77 in 3D Show helices and sheets RCSB PDB PDBe
3A77 contains 44 α-helices and 60 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 | 191-195 | 5 | |
| α-helix | 201 | 1 | |
| β-strand | 202 | 1 | 1 |
| β-strand | 203-210 | 8 | 2 |
| β-strand | 213-221 | 9 | 2 |
| β-strand | 226-228 | 3 | 3 |
| β-strand | 241-243 | 3 | 3 |
| α-helix | 244-247 | 4 | |
| α-helix | 248-250 | 3 | |
| α-helix | 255-267 | 13 | |
| β-strand | 272-277 | 6 | 3 |
| β-strand | 280-285 | 6 | 3 |
| β-strand | 291-296 | 6 | 2 |
| α-helix | 300-302 | 3 | |
| β-strand | 309-310 | 2 | 2 |
| β-strand | 317-321 | 5 | 3 |
| α-helix | 322-333 | 12 | |
| α-helix | 338-341 | 4 | |
| β-strand | 343-348 | 6 | 2 |
| α-helix | 357-360 | 4 | |
| β-strand | 363-369 | 7 | 2 |
| α-helix | 370-383 | 14 | |
| β-strand | 389-391 | 3 | 4 |
| β-strand | 395 | 1 | 1 |
| β-strand | 401-403 | 3 | 4 |
| α-helix | 405-416 | 12 | |
| α-helix | 422-423 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 191-195 | 5 | |
| α-helix | 201 | 1 | |
| β-strand | 202 | 1 | 5 |
| β-strand | 203-210 | 8 | 6 |
| β-strand | 213-221 | 9 | 6 |
| β-strand | 226-229 | 4 | 7 |
| β-strand | 241-244 | 4 | 7 |
| α-helix | 245-247 | 3 | |
| α-helix | 248-250 | 3 | |
| α-helix | 255-267 | 13 | |
| β-strand | 272-277 | 6 | 7 |
| β-strand | 280-285 | 6 | 7 |
| β-strand | 291-296 | 6 | 6 |
| α-helix | 300-302 | 3 | |
| β-strand | 309-310 | 2 | 6 |
| β-strand | 317-321 | 5 | 7 |
| α-helix | 322-333 | 12 | |
| α-helix | 338-341 | 4 | |
| β-strand | 343-348 | 6 | 6 |
| β-strand | 363-369 | 7 | 6 |
| α-helix | 370-382 | 13 | |
| β-strand | 389-391 | 3 | 8 |
| β-strand | 395 | 1 | 5 |
| β-strand | 401-403 | 3 | 8 |
| α-helix | 405-416 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 191-195 | 5 | |
| α-helix | 201 | 1 | |
| β-strand | 202 | 1 | 9 |
| α-helix | 203 | 1 | |
| β-strand | 204-210 | 7 | 10 |
| β-strand | 213-220 | 8 | 10 |
| β-strand | 226-229 | 4 | 11 |
| β-strand | 241-244 | 4 | 11 |
| α-helix | 245-247 | 3 | |
| α-helix | 248-250 | 3 | |
| α-helix | 255-267 | 13 | |
| β-strand | 272-277 | 6 | 11 |
| β-strand | 280-285 | 6 | 11 |
| β-strand | 291-296 | 6 | 10 |
| α-helix | 300-302 | 3 | |
| β-strand | 309-310 | 2 | 10 |
| β-strand | 317-321 | 5 | 11 |
| α-helix | 322-333 | 12 | |
| α-helix | 338-341 | 4 | |
| β-strand | 343-348 | 6 | 10 |
| α-helix | 357-360 | 4 | |
| β-strand | 363-369 | 7 | 10 |
| α-helix | 370-382 | 13 | |
| β-strand | 388-391 | 4 | 12 |
| β-strand | 395 | 1 | 9 |
| β-strand | 401-404 | 4 | 12 |
| α-helix | 405-417 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 191-195 | 5 | |
| α-helix | 200-201 | 2 | |
| β-strand | 202 | 1 | 13 |
| β-strand | 203-210 | 8 | 14 |
| β-strand | 213-221 | 9 | 14 |
| β-strand | 226-229 | 4 | 15 |
| β-strand | 241-244 | 4 | 15 |
| α-helix | 245-247 | 3 | |
| α-helix | 248-250 | 3 | |
| α-helix | 255-267 | 13 | |
| β-strand | 272-277 | 6 | 15 |
| β-strand | 280-285 | 6 | 15 |
| β-strand | 291-296 | 6 | 14 |
| α-helix | 300-302 | 3 | |
| β-strand | 309-310 | 2 | 14 |
| β-strand | 317-321 | 5 | 15 |
| α-helix | 322-333 | 12 | |
| α-helix | 338-341 | 4 | |
| β-strand | 343-348 | 6 | 14 |
| β-strand | 363-369 | 7 | 14 |
| α-helix | 370-380 | 11 | |
| β-strand | 389-391 | 3 | 16 |
| β-strand | 395 | 1 | 13 |
| β-strand | 401-403 | 3 | 16 |
| α-helix | 405-417 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interferon regulatory factor 3 | A, B, C, D | protein | 242 | Homo sapiens | Q14653 (AlphaFold model) |
>3A77_1 Interferon regulatory factor 3 (chains A, B, C, D) GAMENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTL PDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGH GPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMV KVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPG ES
Ser386 phosphorylation of transcription factor IRF-3 induces dimerization and association with CBP/p300 without overall conformational change. Takahasi, K., Horiuchi, M., Fujii, K. et al. Genes Cells (2010) 15:901-910. DOI 10.1111/j.1365-2443.2010.01427.x · PubMed
Other PDB entries of the same protein (UniProt Q14653 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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