1KBH: Nuclear receptor coactivator

Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR. Determined by solution NMR. Released 6 Feb 2002.

Method
Solution NMR
Organisms
Homo sapiens, Mus musculus
Chains
2
Atoms
818
Mol. weight
11.67 kDa
Released
6 Feb 2002

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

Secondary structure: helices and β-sheets

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.

Chain A: 4 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix5-1612
α-helix25-317
α-helix34-407
α-helix42-443
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix56-6510
α-helix75-806
α-helix84-9916

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
nuclear receptor coactivatorAprotein47Homo sapiensQ9Y6Q9 (AlphaFold model)
Creb-binding proteinBprotein59Mus musculusP45481 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1KBH_1 nuclear receptor coactivator (chains A)
EGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPK
Sequence of entity 2 (B), FASTA
>1KBH_2 CREB-BINDING PROTEIN (chains B)
PNRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQ

Primary citation

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:

Browse structure collections

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