Crystal structure of YLGV mutant of dimerisation domain of NF-kB p50 transcription factor. Determined by X-ray diffraction at 2.2 Å resolution. Released 17 Aug 2004.
Explore 1U41 in 3D Show helices and sheets RCSB PDB PDBe
1U41 contains 11 α-helices and 45 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 |
|---|---|---|---|
| β-strand | 250-253 | 4 | 1 |
| β-strand | 257-259 | 3 | 2 |
| β-strand | 265-270 | 6 | 1 |
| β-strand | 281-286 | 6 | 2 |
| β-strand | 290-295 | 6 | 2 |
| β-strand | 297 | 1 | 1 |
| α-helix | 300-302 | 3 | |
| β-strand | 303 | 1 | 1 |
| β-strand | 308-312 | 5 | 1 |
| α-helix | 313-316 | 4 | |
| β-strand | 325-330 | 6 | 2 |
| β-strand | 332 | 1 | 3 |
| β-strand | 339 | 1 | 3 |
| α-helix | 340-342 | 3 | |
| β-strand | 343-348 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 250-253 | 4 | 4 |
| β-strand | 257-259 | 3 | 5 |
| β-strand | 265-270 | 6 | 4 |
| β-strand | 279-285 | 7 | 5 |
| β-strand | 291-295 | 5 | 5 |
| β-strand | 297 | 1 | 4 |
| α-helix | 300-302 | 3 | |
| β-strand | 303 | 1 | 4 |
| β-strand | 308-312 | 5 | 4 |
| α-helix | 313-316 | 4 | |
| β-strand | 325-332 | 8 | 5 |
| β-strand | 339 | 1 | 5 |
| β-strand | 343-348 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 250-253 | 4 | 6 |
| β-strand | 257-259 | 3 | 7 |
| β-strand | 265-270 | 6 | 6 |
| β-strand | 278-283 | 6 | 7 |
| β-strand | 293-295 | 3 | 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 | 325-333 | 9 | 7 |
| β-strand | 339 | 1 | 7 |
| α-helix | 340-342 | 3 | |
| β-strand | 343-348 | 6 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 250-253 | 4 | 8 |
| β-strand | 257-259 | 3 | 9 |
| β-strand | 265-270 | 6 | 8 |
| β-strand | 279-285 | 7 | 9 |
| β-strand | 291-295 | 5 | 9 |
| β-strand | 297 | 1 | 8 |
| α-helix | 300-302 | 3 | |
| β-strand | 303-304 | 2 | 8 |
| β-strand | 308-312 | 5 | 8 |
| α-helix | 313-316 | 4 | |
| β-strand | 325-332 | 8 | 9 |
| β-strand | 339 | 1 | 9 |
| α-helix | 340-342 | 3 | |
| β-strand | 343-348 | 6 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear factor NF-kappa-B p105 subunit | A, B, C, D | protein | 106 | Mus musculus | P25799 (AlphaFold model) |
>1U41_1 Nuclear factor NF-kappa-B p105 subunit (chains A, B, C, D) ASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVH RQFGIVFKTPKYKDVNITKPASVFVQLRRKSDLETSEPKPFLYYPE
Snapshot of Protein Structure Evolution Reveals Conservation of Functional Dimerization through Intertwined Folding. Chirgadze, D.Y., Demydchuk, M., Becker, M. et al. Structure (2004) 12:1489-1494. DOI 10.1016/j.str.2004.06.011 · 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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