Murine NF-kappaB p50 Rel Homology Region homodimer in complex with 10-mer kappaB DNA from human Neutrophil Gelatinase-associated Lipocalin (NGAL) promoter. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Oct 2023.
Explore 8TKN in 3D Show helices and sheets RCSB PDB PDBe
8TKN contains 32 α-helices and 57 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 41-46 | 6 | 1 |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 2 |
| α-helix | 49 | 1 | |
| β-strand | 53 | 1 | 3 |
| β-strand | 56-57 | 2 | 4 |
| α-helix | 58-60 | 3 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69 | 1 | 2 |
| β-strand | 81-85 | 5 | 1 |
| β-strand | 91-98 | 8 | 5 |
| β-strand | 106 | 1 | 5 |
| β-strand | 110-113 | 4 | 4 |
| β-strand | 116-117 | 2 | 5 |
| β-strand | 119 | 1 | 4 |
| β-strand | 120-125 | 6 | 5 |
| α-helix | 126 | 1 | |
| β-strand | 131-133 | 3 | 1 |
| β-strand | 137-141 | 5 | 4 |
| α-helix | 147-161 | 15 | |
| α-helix | 165-168 | 4 | |
| α-helix | 190-203 | 14 | |
| β-strand | 209-210 | 2 | 6 |
| β-strand | 211-218 | 8 | 5 |
| β-strand | 227-228 | 2 | 5 |
| α-helix | 229-231 | 3 | |
| β-strand | 232-233 | 2 | 5 |
| α-helix | 235-236 | 2 | |
| β-strand | 237-238 | 2 | 6 |
| β-strand | 239 | 1 | 3 |
| α-helix | 243-245 | 3 | |
| α-helix | 247-248 | 2 | |
| β-strand | 250-253 | 4 | 7 |
| β-strand | 257-259 | 3 | 8 |
| β-strand | 265-270 | 6 | 7 |
| β-strand | 278-284 | 7 | 8 |
| α-helix | 290-291 | 2 | |
| β-strand | 292-295 | 4 | 8 |
| β-strand | 297 | 1 | 7 |
| α-helix | 300-302 | 3 | |
| β-strand | 303 | 1 | 7 |
| β-strand | 308-312 | 5 | 7 |
| α-helix | 313-316 | 4 | |
| α-helix | 324 | 1 | |
| β-strand | 325-333 | 9 | 8 |
| β-strand | 339 | 1 | 8 |
| β-strand | 343-348 | 6 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 41-46 | 6 | 9 |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 10 |
| α-helix | 49 | 1 | |
| β-strand | 56 | 1 | 11 |
| α-helix | 58-60 | 3 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69 | 1 | 10 |
| β-strand | 81-85 | 5 | 9 |
| β-strand | 91-98 | 8 | 12 |
| α-helix | 105 | 1 | |
| β-strand | 106 | 1 | 12 |
| α-helix | 107 | 1 | |
| β-strand | 110-113 | 4 | 11 |
| β-strand | 116-117 | 2 | 12 |
| β-strand | 120-125 | 6 | 12 |
| β-strand | 131-133 | 3 | 9 |
| β-strand | 137-140 | 4 | 11 |
| α-helix | 141-143 | 3 | |
| α-helix | 144-146 | 3 | |
| α-helix | 147-160 | 14 | |
| α-helix | 165-168 | 4 | |
| α-helix | 171-173 | 3 | |
| α-helix | 190-204 | 15 | |
| β-strand | 209-219 | 11 | 12 |
| β-strand | 225-228 | 4 | 12 |
| β-strand | 232-238 | 7 | 12 |
| α-helix | 247-248 | 2 | |
| β-strand | 250-253 | 4 | 13 |
| β-strand | 257-259 | 3 | 14 |
| β-strand | 265-270 | 6 | 13 |
| α-helix | 275-277 | 3 | |
| β-strand | 279-286 | 8 | 14 |
| β-strand | 289-295 | 7 | 14 |
| β-strand | 297 | 1 | 13 |
| α-helix | 300-302 | 3 | |
| β-strand | 303-304 | 2 | 13 |
| β-strand | 308-312 | 5 | 13 |
| α-helix | 313-316 | 4 | |
| β-strand | 325-332 | 8 | 14 |
| β-strand | 339 | 1 | 14 |
| β-strand | 343-348 | 6 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear factor NF-kappa-B p50 subunit | A, B | protein | 312 | Mus musculus | P25799 (AlphaFold model) |
| DNA a | C, E | DNA | 10 | Homo sapiens | |
| DNA B | D, F | DNA | 10 | Homo sapiens |
>8TKN_1 Nuclear factor NF-kappa-B p50 subunit (chains A, B) GPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLV TNGKNIHLHAHSLVGKHCEDGVCTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEA CIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAAVQQTKEMDLSVVRLMFTAFL PDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDI QIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASVFVQLRRKSDLE TSEPKPFLYYPE
>8TKN_2 DNA A (chains C, E) GGGAATGTCC
>8TKN_3 DNA B (chains D, F) GGACATTCCC
X-ray Crystallographic Study of Preferred Spacing by the NF-kappa B p50 Homodimer on kappa B DNA. Zhu, N., Mealka, M., Mitchel, S. et al. Biomolecules (2023) 13. DOI 10.3390/biom13091310 · PubMed
Other PDB entries of the same protein (UniProt P25799 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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