1U42: Nuclear factor NF-kappa-B p105 subunit

Crystal structure of MLAM mutant of dimerisation domain of NF-kB p50 transcription factor. Determined by X-ray diffraction at 2.7 Å resolution. Released 17 Aug 2004.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Mus musculus
Chains
1
Atoms
814
Mol. weight
12.26 kDa
Released
17 Aug 2004

Explore 1U42 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1U42 contains 1 α-helix and 8 β-strands across 1 chain. 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: 1 helix, 8 β-strands

ElementResiduesLengthSheet
β-strand252-25321
β-strand268-26921
β-strand281-28442
β-strand292-29542
α-helix313-3164
β-strand325-32953
β-strand33214
β-strand33914
β-strand343-34753

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Nuclear factor NF-kappa-B p105 subunitAprotein106Mus musculusP25799 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1U42_1 Nuclear factor NF-kappa-B p105 subunit (chains A)
ASNLKIVRMDRTAGCVTGGEEIMLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVH
RQFAIMFKTPKYKDVNITKPASVFVQLRRKSDLETSEPKPFLYYPE

Primary citation

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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