Crystal structure of nf-kB(p50)2 complexed to a high-affinity RNA aptamer. Determined by X-ray diffraction at 2.45 Å resolution. Released 22 Jul 2003.
Explore 1OOA in 3D Show helices and sheets RCSB PDB PDBe
1OOA contains 26 α-helices and 56 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 |
| α-helix | 54-55 | 2 | |
| β-strand | 56 | 1 | 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 | 120-125 | 6 | 5 |
| β-strand | 131-133 | 3 | 1 |
| β-strand | 137-140 | 4 | 4 |
| α-helix | 144-146 | 3 | |
| α-helix | 147-161 | 15 | |
| α-helix | 165-168 | 4 | |
| α-helix | 171-173 | 3 | |
| α-helix | 188-202 | 15 | |
| β-strand | 209-219 | 11 | 5 |
| β-strand | 225-228 | 4 | 5 |
| β-strand | 232-238 | 7 | 5 |
| β-strand | 239 | 1 | 3 |
| β-strand | 250-253 | 4 | 6 |
| β-strand | 257-259 | 3 | 7 |
| β-strand | 265-270 | 6 | 6 |
| β-strand | 279-285 | 7 | 7 |
| β-strand | 291-295 | 5 | 7 |
| β-strand | 297 | 1 | 6 |
| α-helix | 300-302 | 3 | |
| β-strand | 303 | 1 | 6 |
| β-strand | 308-312 | 5 | 6 |
| α-helix | 313-316 | 4 | |
| β-strand | 325-332 | 8 | 7 |
| β-strand | 339 | 1 | 7 |
| α-helix | 340-342 | 3 | |
| β-strand | 343-348 | 6 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 41-46 | 6 | 8 |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 9 |
| α-helix | 49 | 1 | |
| β-strand | 53 | 1 | 10 |
| α-helix | 54-55 | 2 | |
| β-strand | 56 | 1 | 11 |
| α-helix | 58-60 | 3 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69 | 1 | 9 |
| β-strand | 81-85 | 5 | 8 |
| β-strand | 92-98 | 7 | 12 |
| β-strand | 106 | 1 | 12 |
| β-strand | 110-113 | 4 | 11 |
| β-strand | 116-117 | 2 | 12 |
| β-strand | 120-124 | 5 | 12 |
| β-strand | 131-133 | 3 | 8 |
| β-strand | 137-140 | 4 | 11 |
| α-helix | 147-160 | 14 | |
| α-helix | 165-168 | 4 | |
| α-helix | 171-173 | 3 | |
| α-helix | 188-202 | 15 | |
| β-strand | 209-219 | 11 | 12 |
| β-strand | 225-228 | 4 | 12 |
| β-strand | 232-238 | 7 | 12 |
| β-strand | 239 | 1 | 10 |
| α-helix | 242-244 | 3 | |
| β-strand | 250-253 | 4 | 13 |
| β-strand | 257-259 | 3 | 14 |
| β-strand | 265-270 | 6 | 13 |
| β-strand | 279-285 | 7 | 14 |
| β-strand | 291-295 | 5 | 14 |
| β-strand | 297 | 1 | 13 |
| α-helix | 300-302 | 3 | |
| β-strand | 303 | 1 | 13 |
| β-strand | 308-312 | 5 | 13 |
| α-helix | 313-316 | 4 | |
| β-strand | 325-332 | 8 | 14 |
| β-strand | 339 | 1 | 14 |
| α-helix | 340-342 | 3 | |
| β-strand | 343-348 | 6 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA aptamer | C, D | RNA | 29 | ||
| Nuclear factor NF-kappa-B p105 subunit | A, B | protein | 326 | Mus musculus | P25799 (AlphaFold model) |
>1OOA_1 RNA aptamer (chains C, D) CAUACUUGAAACUGUAAGGUUGGCGUAUG
>1OOA_2 Nuclear factor NF-kappa-B p105 subunit (chains A, B) GGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQL VTNGKNIHLHAHSLVGKHCEDGVCTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTE ACIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAAVQQTKEMDLSVVRLMFTAF LPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDD IQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASVFVQLRRKSDL ETSEPKPFLYYPEIKDKEEVQRKRQK
Crystal structure of NF-kappaB (p50)2 complexed to a high-affinity RNA aptamer. Huang, D.B., Vu, D., Cassiday, L.A. et al. Proc Natl Acad Sci U S A (2003) 100:9268-9273. DOI 10.1073/pnas.1632011100 · 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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