Structure of NF-kB p52 homodimer bound to +1/-1 swap P-Selectin kB DNA fragment. Determined by X-ray diffraction at 3.4 Å resolution. Released 24 Nov 2021.
Explore 7VUP in 3D Show helices and sheets RCSB PDB PDBe
7VUP contains 20 α-helices and 60 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 | 39-44 | 6 | 1 |
| α-helix | 45 | 1 | |
| β-strand | 46 | 1 | 2 |
| α-helix | 47 | 1 | |
| β-strand | 51 | 1 | 3 |
| α-helix | 52-53 | 2 | |
| β-strand | 54-55 | 2 | 4 |
| β-strand | 67 | 1 | 2 |
| β-strand | 79-83 | 5 | 1 |
| β-strand | 89-96 | 8 | 5 |
| α-helix | 103 | 1 | |
| β-strand | 104 | 1 | 5 |
| α-helix | 105 | 1 | |
| β-strand | 108-110 | 3 | 4 |
| β-strand | 114 | 1 | 5 |
| β-strand | 120-124 | 5 | 5 |
| β-strand | 130-132 | 3 | 1 |
| β-strand | 137-140 | 4 | 4 |
| α-helix | 141-142 | 2 | |
| α-helix | 146-157 | 12 | |
| α-helix | 168-182 | 15 | |
| β-strand | 189-190 | 2 | 6 |
| β-strand | 191-198 | 8 | 5 |
| β-strand | 207-208 | 2 | 5 |
| β-strand | 212-213 | 2 | 5 |
| α-helix | 214-216 | 3 | |
| β-strand | 217-218 | 2 | 6 |
| β-strand | 219 | 1 | 3 |
| β-strand | 230-233 | 4 | 7 |
| β-strand | 237-239 | 3 | 8 |
| β-strand | 245-250 | 6 | 7 |
| β-strand | 259-263 | 5 | 8 |
| β-strand | 271-273 | 3 | 8 |
| β-strand | 275 | 1 | 7 |
| α-helix | 278-280 | 3 | |
| β-strand | 281-282 | 2 | 7 |
| β-strand | 286-290 | 5 | 7 |
| α-helix | 291-294 | 4 | |
| β-strand | 303-310 | 8 | 8 |
| β-strand | 317 | 1 | 8 |
| β-strand | 321-326 | 6 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 39-44 | 6 | 9 |
| α-helix | 45 | 1 | |
| β-strand | 46 | 1 | 10 |
| α-helix | 47 | 1 | |
| β-strand | 51 | 1 | 11 |
| α-helix | 52-53 | 2 | |
| β-strand | 54-55 | 2 | 12 |
| β-strand | 67 | 1 | 10 |
| β-strand | 79-83 | 5 | 9 |
| β-strand | 89-96 | 8 | 13 |
| β-strand | 104 | 1 | 13 |
| β-strand | 108-110 | 3 | 12 |
| β-strand | 114 | 1 | 13 |
| β-strand | 120-124 | 5 | 13 |
| β-strand | 130-132 | 3 | 9 |
| β-strand | 137-140 | 4 | 12 |
| α-helix | 141-142 | 2 | |
| α-helix | 146-157 | 12 | |
| α-helix | 168-182 | 15 | |
| β-strand | 189-190 | 2 | 14 |
| β-strand | 191-198 | 8 | 13 |
| β-strand | 207-208 | 2 | 13 |
| β-strand | 212-213 | 2 | 13 |
| α-helix | 214-216 | 3 | |
| β-strand | 217-218 | 2 | 14 |
| β-strand | 219 | 1 | 11 |
| β-strand | 230-233 | 4 | 15 |
| β-strand | 237-239 | 3 | 16 |
| β-strand | 245-250 | 6 | 15 |
| β-strand | 258-263 | 6 | 16 |
| β-strand | 271-273 | 3 | 16 |
| β-strand | 275 | 1 | 15 |
| α-helix | 278-280 | 3 | |
| β-strand | 281-282 | 2 | 15 |
| β-strand | 286-290 | 5 | 15 |
| α-helix | 291-294 | 4 | |
| β-strand | 303-311 | 9 | 16 |
| β-strand | 317 | 1 | 16 |
| β-strand | 321-326 | 6 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear factor NF-kappa-B p52 subunit | A, B | protein | 398 | Homo sapiens | Q00653 (AlphaFold model) |
| DNA (5'-d(*cp*ap*ap*gp*gp*gp*gp*ap*cp*tp*cp*cp*cp*cp*cp*tp*t)-3') | C | DNA | 18 | Homo sapiens | |
| DNA (5'-d(*ap*ap*gp*gp*gp*gp*gp*ap*gp*tp*cp*cp*cp*cp*tp*tp*g)-3') | D | DNA | 18 | Homo sapiens |
>7VUP_1 Nuclear factor NF-kappa-B p52 subunit (chains A, B) MESCYNPGLDGIIEYDDFKLNSSIVEPKEPAPETADGPYLVIVEQPKQRGFRFRYGCEGP SHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSELGIC AVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRPQGLTEAEQRELEQEAKE LKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSKSPGASNLKISRMDKTAGSV RGGDEVYLLCDKVQKDDIEVRFYEDDENGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIE RPVTVFLQLKRKRGGDVSDSKQFTYYPLVEDKEEVQRKRRKALPTFSQPFGGGSHMGGGS GGAAGGYGGAGGGGSLGFFPSSLAYSPYQSGAGPMGCY
>7VUP_2 DNA (5'-D(*CP*AP*AP*GP*GP*GP*GP*AP*CP*TP*CP*CP*CP*CP*CP*TP*T)-3') (chains C) CAAGGGGACTCCCCCTTC
>7VUP_3 DNA (5'-D(*AP*AP*GP*GP*GP*GP*GP*AP*GP*TP*CP*CP*CP*CP*TP*TP*G)-3') (chains D) GAAGGGGGAGTCCCCTTG
Structures of NF-kappa B p52 homodimer-DNA complexes rationalize binding mechanisms and transcription activation. Pan, W., Meshcheryakov, V.A., Li, T. et al. Elife (2023) 12. DOI 10.7554/eLife.86258 · PubMed
Other PDB entries of the same protein (UniProt Q00653 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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