Hat domain of GCN5 from saccharomyces cerevisiae. Determined by X-ray diffraction at 1.9 Å resolution. Released 2 Aug 1999.
Explore 1YGH in 3D Show helices and sheets RCSB PDB PDBe
1YGH contains 16 α-helices and 16 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 |
|---|---|---|---|
| β-strand | 100-105 | 6 | 1 |
| α-helix | 111-127 | 17 | |
| α-helix | 133-141 | 9 | |
| β-strand | 146-152 | 7 | 1 |
| β-strand | 156-166 | 11 | 1 |
| α-helix | 167-169 | 3 | |
| β-strand | 171-179 | 9 | 1 |
| α-helix | 188-203 | 16 | |
| β-strand | 208-213 | 6 | 1 |
| α-helix | 215-217 | 3 | |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 1 |
| α-helix | 234-237 | 4 | |
| β-strand | 238 | 1 | 2 |
| β-strand | 241 | 1 | 2 |
| β-strand | 248-253 | 6 | 1 |
| α-helix | 255-257 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 100-105 | 6 | 3 |
| α-helix | 111-127 | 17 | |
| α-helix | 133-141 | 9 | |
| β-strand | 146-152 | 7 | 3 |
| β-strand | 156-166 | 11 | 3 |
| α-helix | 167-169 | 3 | |
| β-strand | 171-179 | 9 | 3 |
| α-helix | 188-203 | 16 | |
| β-strand | 208-213 | 6 | 3 |
| α-helix | 215-217 | 3 | |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 3 |
| α-helix | 234-237 | 4 | |
| β-strand | 248-253 | 6 | 3 |
| α-helix | 255-257 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (transcriptional activator GCN5) | A, B | protein | 164 | Saccharomyces cerevisiae | Q03330 (AlphaFold model) |
>1YGH_1 PROTEIN (TRANSCRIPTIONAL ACTIVATOR GCN5) (chains A, B) KIEFRVVNNDNTKENMMVLTGLKNIFQKQLPKMPKEYIARLVYDRSHLSMAVIRKPLTVV GGITYRPFDKREFAEIVFCAISSTEQVRGYGAHLMNHLKDYVRNTSNIKYFLTYADNYAI GYFKKQGFTKEITLDKSIWMGYIKDYEGGTLMQCSMLPRIRYLD
Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Trievel, R.C., Rojas, J.R., Sterner, D.E. et al. Proc Natl Acad Sci U S A (1999) 96:8931-8936. DOI 10.1073/pnas.96.16.8931 · 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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