Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins. Determined by solution NMR. Released 31 Oct 2018.
Explore 6ES7 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1044-1056 | 13 | |
| α-helix | 1061-1071 | 11 | |
| α-helix | 1075-1078 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2064-2075 | 12 | |
| α-helix | 2081-2092 | 12 | |
| α-helix | 2094-2102 | 9 | |
| α-helix | 2104-2107 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear receptor coactivator 3 | A | protein | 44 | Homo sapiens | Q9Y6Q9 (AlphaFold model) |
| CREB-binding protein | B | protein | 50 | Homo sapiens | Q92793 (AlphaFold model) |
>6ES7_1 Nuclear receptor coactivator 3 (chains A) GSEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQ
>6ES7_2 CREB-binding protein (chains B) GSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYV
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:
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