BRD3-BD1 in complex with RaPID linear peptide 3xAcK.1 (triAcK.1). Determined by X-ray diffraction at 1.41 Å resolution. Released 25 Jan 2023.
Explore 7TOA in 3D Show helices and sheets RCSB PDB PDBe
7TOA contains 17 α-helices and 4 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 36 | 1 | 2 |
| α-helix | 37-41 | 5 | |
| α-helix | 42-47 | 6 | |
| α-helix | 48-51 | 4 | |
| α-helix | 57-59 | 3 | |
| α-helix | 73-76 | 4 | |
| α-helix | 83-91 | 9 | |
| α-helix | 98-115 | 18 | |
| α-helix | 121-138 | 18 | |
| β-strand | 146 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 36 | 1 | 1 |
| α-helix | 37-41 | 5 | |
| α-helix | 42-47 | 6 | |
| α-helix | 48-52 | 5 | |
| α-helix | 57-59 | 3 | |
| α-helix | 73-76 | 4 | |
| α-helix | 83-91 | 9 | |
| α-helix | 98-115 | 18 | |
| α-helix | 121-138 | 18 | |
| β-strand | 146 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-12 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bromodomain-containing protein 3 | A, B | protein | 116 | Homo sapiens | Q15059 (AlphaFold model) |
| 3xAcK.1 (triAcK.1) | D | protein | 11 | synthetic construct |
>7TOA_1 Bromodomain-containing protein 3 (chains A, B) PGRKTNQLQYMQNVVVKTLWKHQFAWPFYQPVDAIKLNLPDYHKIIKNPMDMGTIKKRLE NNYYWSASECMQDFNTMFTNCYIYNKPTDDIVLMAQALEKIFLQKVAQMPQEEVEL
>7TOA_2 3xAcK.1 (triAcK.1) (chains D) RSLKLLKHLKH
mRNA display reveals a class of high-affinity bromodomain-binding motifs that are not found in the human proteome. Low, J.K.K., Patel, K., Jones, N. et al. J Biol Chem (2023) 299:105482-105482. DOI 10.1016/j.jbc.2023.105482 · PubMed
Other PDB entries of the same protein (UniProt Q15059 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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