Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4 Peptide. Determined by X-ray diffraction at 2.25 Å resolution. Released 3 Aug 2004.
Explore 1Q2C in 3D Show helices and sheets RCSB PDB PDBe
1Q2C contains 6 α-helices and 7 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 |
|---|---|---|---|
| β-strand | 50-54 | 5 | 1 |
| α-helix | 60-76 | 17 | |
| α-helix | 82-90 | 9 | |
| β-strand | 94-101 | 8 | 1 |
| β-strand | 105-115 | 11 | 1 |
| β-strand | 120-128 | 9 | 1 |
| α-helix | 130-132 | 3 | |
| α-helix | 137-151 | 15 | |
| β-strand | 156-161 | 6 | 1 |
| α-helix | 164-171 | 8 | |
| β-strand | 175 | 1 | 1 |
| α-helix | 182-184 | 3 | |
| β-strand | 196-201 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| histone acetyltransferase GCN5 | A | protein | 162 | Tetrahymena thermophila | Q27198 (AlphaFold model) |
| Histone H4 peptide | B | protein | 19 |
>1Q2C_1 histone acetyltransferase GCN5 (chains A) LDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQKVIG GICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNFAIGY FKKQGFTKEHRMPQEKWKGYIKDYDGGTLMECYIHPYVDYGR
>1Q2C_2 Histone H4 peptide (chains B) SGRGKGGKGLGKGGAKRHR
| ID | Name | Formula | Copies |
|---|---|---|---|
| COA | Coenzyme a | C21 H36 N7 O16 P3 S | 1 |
Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase. Clements, A., Poux, A.N., Lo, S. et al. Mol Cell (2003) 12:461-473. DOI 10.1016/S1097-2765(03)00288-0 · PubMed
Other PDB entries of the same protein (UniProt Q27198 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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