5JEM: Complex of IRF-3 with CBP
Complex of IRF-3 with CBP. Determined by X-ray diffraction at 2.5 Å resolution. Released 15 Jun 2016.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 7,872
- Mol. weight
- 116.2 kDa
- Released
- 15 Jun 2016
Explore 5JEM in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5JEM contains 41 α-helices and 54 β-strands across 8 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.
Chain A: 7 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 203-210 | 8 | 1 |
| β-strand | 213-221 | 9 | 1 |
| β-strand | 226-229 | 4 | 2 |
| β-strand | 241-244 | 4 | 2 |
| α-helix | 245-247 | 3 | |
| α-helix | 248-250 | 3 | |
| α-helix | 255-266 | 12 | |
| β-strand | 272-277 | 6 | 2 |
| β-strand | 280-285 | 6 | 2 |
| β-strand | 289 | 1 | 3 |
| β-strand | 291-296 | 6 | 1 |
| β-strand | 309-310 | 2 | 1 |
| β-strand | 317-321 | 5 | 2 |
| α-helix | 322-333 | 12 | |
| α-helix | 339-341 | 3 | |
| β-strand | 343-348 | 6 | 1 |
| α-helix | 358-360 | 3 | |
| β-strand | 363-369 | 7 | 1 |
| α-helix | 370-382 | 13 | |
| β-strand | 395 | 1 | 4 |
Chain B: 7 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 203-210 | 8 | 5 |
| β-strand | 213-221 | 9 | 5 |
| β-strand | 226-229 | 4 | 6 |
| β-strand | 241-244 | 4 | 6 |
| α-helix | 245-247 | 3 | |
| α-helix | 248-250 | 3 | |
| α-helix | 255-266 | 12 | |
| β-strand | 272-277 | 6 | 6 |
| β-strand | 280-285 | 6 | 6 |
| β-strand | 289 | 1 | 4 |
| β-strand | 291-296 | 6 | 5 |
| β-strand | 309-310 | 2 | 5 |
| β-strand | 317-321 | 5 | 6 |
| α-helix | 322-333 | 12 | |
| α-helix | 339-341 | 3 | |
| β-strand | 343-348 | 6 | 5 |
| α-helix | 358-360 | 3 | |
| β-strand | 364-369 | 6 | 5 |
| α-helix | 370-382 | 13 | |
| β-strand | 395 | 1 | 3 |
Chains C and F: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2066-2072 | 7 | |
| α-helix | 2080-2092 | 13 | |
| α-helix | 2094-2104 | 11 | |
Chain D: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2066-2071 | 6 | |
| α-helix | 2080-2091 | 12 | |
| α-helix | 2094-2104 | 11 | |
Chain E: 7 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 202-210 | 9 | 7 |
| β-strand | 213-222 | 10 | 7 |
| β-strand | 226-229 | 4 | 8 |
| β-strand | 241-244 | 4 | 8 |
| α-helix | 245-247 | 3 | |
| α-helix | 248-250 | 3 | |
| α-helix | 255-266 | 12 | |
| β-strand | 272-277 | 6 | 8 |
| β-strand | 280-285 | 6 | 8 |
| β-strand | 289 | 1 | 9 |
| β-strand | 291-296 | 6 | 7 |
| β-strand | 309-310 | 2 | 7 |
| β-strand | 317-321 | 5 | 8 |
| α-helix | 322-333 | 12 | |
| α-helix | 339-341 | 3 | |
| β-strand | 343-348 | 6 | 7 |
| α-helix | 358-360 | 3 | |
| β-strand | 363-369 | 7 | 7 |
| α-helix | 370-381 | 12 | |
| β-strand | 393 | 1 | 10 |
| β-strand | 395 | 1 | 11 |
Chain G: 8 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 202-210 | 9 | 12 |
| β-strand | 213-222 | 10 | 12 |
| β-strand | 226-229 | 4 | 13 |
| β-strand | 241-244 | 4 | 13 |
| α-helix | 245-247 | 3 | |
| α-helix | 248-250 | 3 | |
| α-helix | 255-266 | 12 | |
| β-strand | 272-277 | 6 | 13 |
| β-strand | 280-285 | 6 | 13 |
| β-strand | 289 | 1 | 11 |
| β-strand | 291-296 | 6 | 12 |
| β-strand | 309-310 | 2 | 12 |
| α-helix | 311-312 | 2 | |
| β-strand | 317-321 | 5 | 13 |
| α-helix | 322-333 | 12 | |
| α-helix | 339-341 | 3 | |
| β-strand | 343-348 | 6 | 12 |
| β-strand | 350 | 1 | 10 |
| α-helix | 358-360 | 3 | |
| β-strand | 363-369 | 7 | 12 |
| α-helix | 370-382 | 13 | |
| β-strand | 395 | 1 | 9 |
Chain H: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2066-2071 | 6 | |
| α-helix | 2080-2092 | 13 | |
| α-helix | 2094-2104 | 11 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Interferon regulatory factor 3 | A, B, E, G | protein | 213 | Homo sapiens | Q14653 (AlphaFold model) |
| CREB-binding protein | C, D, F, H | protein | 47 | Homo sapiens | Q92793 (AlphaFold model) |
Sequence of entity 1 (A, B, E, G), FASTA
>5JEM_1 Interferon regulatory factor 3 (chains A, B, E, G)
SEFENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTL
PDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGH
GPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMV
KVVPTCLRALVEMARVGGASELENTVDLHIENS
Sequence of entity 2 (C, D, F, H), FASTA
>5JEM_2 CREB-binding protein (chains C, D, F, H)
SALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVAN
Primary citation
Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins. Zhao, B., Shu, C., Gao, X. et al. Proc Natl Acad Sci U S A (2016) 113:E3403-E3412. DOI 10.1073/pnas.1603269113 · PubMed
Other PDB entries of the same protein (UniProt Q14653 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6SJA 1.5 Å, Structure of HPV16 E6 oncoprotein in complex with IRF3 LxxLL motif
- 5JEL 1.6 Å, Phosphorylated TRIF in complex with IRF-3
- 7JFL 1.68 Å, Crystal structure of human phosphorylated IRF-3 bound to CBP
- 5JEO 1.72 Å, Phosphorylated Rotavirus NSP1 in complex with IRF-3
- 6SIV 1.75 Å, Structure of HPV16 E6 oncoprotein in complex with mutant IRF3 LxxLL motif
- 3A77 1.8 Å, The crystal structure of phosphorylated IRF-3
- 5JEJ 2.0 Å, Phosphorylated STING in complex with IRF-3 CTD
- 1QWT 2.1 Å, Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain
- 1J2F 2.3 Å, X-ray crystal structure of IRF-3 and its functional implications
- 3QU6 2.3 Å, Crystal structure of IRF-3 DBD free form
- 2PI0 2.31 Å, Crystal Structure of IRF-3 bound to the PRDIII-I regulatory element of the human…
- 1ZOQ 2.37 Å, IRF3-CBP complex
Browse structure collections
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