Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR. Determined by solution NMR. Released 6 Feb 2002.
Explore 1KBH in 3D Show helices and sheets RCSB PDB PDBe
1KBH contains 7 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 5-16 | 12 | |
| α-helix | 25-31 | 7 | |
| α-helix | 34-40 | 7 | |
| α-helix | 42-44 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 56-65 | 10 | |
| α-helix | 75-80 | 6 | |
| α-helix | 84-99 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| nuclear receptor coactivator | A | protein | 47 | Homo sapiens | Q9Y6Q9 (AlphaFold model) |
| Creb-binding protein | B | protein | 59 | Mus musculus | P45481 (AlphaFold model) |
>1KBH_1 nuclear receptor coactivator (chains A) EGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPK
>1KBH_2 CREB-BINDING PROTEIN (chains B) PNRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQ
Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Demarest, S.J., Martinez-Yamout, M., Chung, J. et al. Nature (2002) 415:549-553. DOI 10.1038/415549a · PubMed
Other PDB entries of the same protein (UniProt Q9Y6Q9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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