Histone acetyltransferase HAT1 from saccharomyces cerevisiae in complex with acetyl coenzyme a. Determined by X-ray diffraction at 2.3 Å resolution. Released 20 Apr 1999.
Explore 1BOB in 3D Show helices and sheets RCSB PDB PDBe
1BOB contains 14 α-helices and 16 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 | 8-10 | 3 | |
| β-strand | 12-14 | 3 | 1 |
| α-helix | 15-18 | 4 | |
| β-strand | 19-24 | 6 | 2 |
| β-strand | 28-31 | 4 | 2 |
| α-helix | 37-40 | 4 | |
| β-strand | 45-47 | 3 | 1 |
| β-strand | 49-50 | 2 | 3 |
| β-strand | 53-59 | 7 | 2 |
| β-strand | 65-70 | 6 | 2 |
| β-strand | 73-74 | 2 | 3 |
| α-helix | 83-88 | 6 | |
| α-helix | 92 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| α-helix | 101-114 | 14 | |
| β-strand | 122-129 | 8 | 4 |
| β-strand | 132-139 | 8 | 4 |
| α-helix | 144-153 | 10 | |
| α-helix | 155-160 | 6 | |
| β-strand | 174-181 | 8 | 4 |
| β-strand | 187-196 | 10 | 4 |
| β-strand | 213-222 | 10 | 4 |
| α-helix | 224-226 | 3 | |
| α-helix | 231-245 | 15 | |
| β-strand | 249-254 | 6 | 4 |
| α-helix | 259-275 | 17 | |
| α-helix | 278-281 | 4 | |
| α-helix | 290-300 | 11 | |
| β-strand | 302 | 1 | 4 |
| α-helix | 304-317 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase | A | protein | 320 | Saccharomyces cerevisiae | Q12341 (AlphaFold model) |
>1BOB_1 HISTONE ACETYLTRANSFERASE (chains A) MSANDFKPETWTSSANEALRVSIVGENAVQFSPLFTYPIYGDSEKIYGYKDLIIHLAFDS VTFKPYVNVKYSAKLGDDNIVDVEKKLLSFLPKDDVIVRDEAKWVDCFAEERKTHNLSDV FEKVSEYSLNGEEFVVYKSSLVDDFARRMHRRVQIFSLLFIEAANYIDETDPSWQIYWLL NKKTKELIGFVTTYKYWHYLGAKSFDEDIDKKFRAKISQFLIFPPYQNKGHGSCLYEAII QSWLEDKSITEITVEDPNEAFDDLRDRNDIQRLRKLGYDAVFQKHSDLSDEFLESSRKSL KLEERQFNRLVEMLLLLNNS
Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Dutnall, R.N., Tafrov, S.T., Sternglanz, R. et al. Cell (1998) 94:427-438. DOI 10.1016/S0092-8674(00)81584-6 · PubMed
Other PDB entries of the same protein (UniProt Q12341 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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