Crystal structure of human Bromodomain containing protein 3 (BRD3) in complex with SHMT. Determined by X-ray diffraction at 1.5 Å resolution. Released 3 Aug 2022.
Explore 7RJL in 3D Show helices and sheets RCSB PDB PDBe
7RJL contains 20 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 | 23-25 | 3 | |
| 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 | |
| α-helix | 140-142 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-36 | 3 | |
| 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 | 121-137 | 17 | |
| α-helix | 140-143 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bromodomain-containing protein 3 | A, B | protein | 123 | Homo sapiens | Q15059 (AlphaFold model) |
| Serine hydroxymethyltransferase, cytosolic | C, D | protein | 6 | Homo sapiens | P34896 (AlphaFold model) |
>7RJL_1 Bromodomain-containing protein 3 (chains A, B) SMPEVSNPSKPGRKTNQLQYMQNVVVKTLWKHQFAWPFYQPVDAIKLNLPDYHKIIKNPM DMGTIKKRLENNYYWSASECMQDFNTMFTNCYIYNKPTDDIVLMAQALEKIFLQKVAQMP QEE
>7RJL_2 Serine hydroxymethyltransferase, cytosolic (chains C, D) RKGVKS
Uncovering the Bromodomain Interactome using Site-Specific Azide-Acetyllysine Photochemistry, Proteomic Profiling and Structural Characterization. Wagner, S., Fedorov, E., Sudhamalla, B. et al. bioRxiv (2021). DOI 10.1101/2021.07.28.453719
Other PDB entries of the same protein (UniProt Q15059 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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