6ES7: Nuclear receptor coactivator 3

Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins. Determined by solution NMR. Released 31 Oct 2018.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
716
Mol. weight
10.24 kDa
Released
31 Oct 2018

Explore 6ES7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6ES7 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: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix1044-105613
α-helix1061-107111
α-helix1075-10784
Chain B: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix2064-207512
α-helix2081-209212
α-helix2094-21029
α-helix2104-21074

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Nuclear receptor coactivator 3Aprotein44Homo sapiensQ9Y6Q9 (AlphaFold model)
CREB-binding proteinBprotein50Homo sapiensQ92793 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6ES7_1 Nuclear receptor coactivator 3 (chains A)
GSEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQ
Sequence of entity 2 (B), FASTA
>6ES7_2 CREB-binding protein (chains B)
GSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYV

Primary citation

Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins. Jemth, P., Karlsson, E., Vogeli, B. et al. Sci Adv (2018) 4:eaau4130-eaau4130. DOI 10.1126/sciadv.aau4130 · 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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