Bromodomain from GCN5 complexed with acetylated H4 peptide. Determined by X-ray diffraction at 1.87 Å resolution. Released 24 Nov 2000.
Explore 1E6I in 3D Show helices and sheets RCSB PDB PDBe
1E6I contains 8 α-helices and 0 β-strands across 1 chain. 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 | 333-345 | 13 | |
| α-helix | 350-352 | 3 | |
| α-helix | 355-357 | 3 | |
| α-helix | 364-367 | 4 | |
| α-helix | 374-382 | 9 | |
| α-helix | 389-406 | 18 | |
| α-helix | 412-429 | 18 | |
| α-helix | 432-437 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcriptional activator GCN5 | A | protein | 121 | SACCHAROMYCES CEREVISIAE | Q03330 (AlphaFold model) |
| Histone H4 | P | protein | 15 | SACCHAROMYCES CEREVISIAE | P02309 (AlphaFold model) |
>1E6I_1 TRANSCRIPTIONAL ACTIVATOR GCN5 (chains A) AMANIAQRPKRGPHDAAIQNILTELQNHAAAWPFLQPVNKEEVPDYYDFIKEPMDLSTME IKLESNKYQKMEDFIYDARLVFNNCRMYNGENTSYYKYANRLEKFFNNKVKEIPEYSHLI D
>1E6I_2 HISTONE H4 (chains P) AKRHRKILRNSIQGI
The Structural Basis for the Recognition of Acetylated Histone H4 by the Bromodomain of Histone Acetyltransferase Gcn5P. Owen, D.J., Ornaghi, P., Yang, J.C. et al. EMBO J (2000) 19:6141. DOI 10.1093/EMBOJ/19.22.6141 · PubMed
Other PDB entries of the same protein (UniProt Q03330 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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