Catalytic domain of tetrahymena GCN5 histone acetyltransferase in complex with coenzyme a. Determined by solution NMR. Released 19 Jul 1999.
Explore 5GCN in 3D Show helices and sheets RCSB PDB PDBe
5GCN contains 6 α-helices and 11 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 | 6-10 | 5 | 1 |
| α-helix | 17-32 | 16 | |
| α-helix | 38-45 | 8 | |
| β-strand | 51-56 | 6 | 1 |
| β-strand | 62-70 | 9 | 1 |
| β-strand | 76 | 1 | 2 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 86-88 | 3 | |
| α-helix | 94-107 | 14 | |
| β-strand | 112 | 1 | 2 |
| β-strand | 115-116 | 2 | 3 |
| α-helix | 119-128 | 10 | |
| β-strand | 131 | 1 | 4 |
| α-helix | 138-141 | 4 | |
| β-strand | 153-154 | 2 | 3 |
| β-strand | 155 | 1 | 4 |
| β-strand | 157 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase GCN5 | A | protein | 166 | Tetrahymena thermophila | Q27198 (AlphaFold model) |
>5GCN_1 HISTONE ACETYLTRANSFERASE GCN5 (chains A) MKGLLDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQ KVIGGICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNF AIGYFKKQGFTKEHRMPQEKWKGYIKDYDGGTLMECYIHPYVDYGN
| ID | Name | Formula | Copies |
|---|---|---|---|
| COA | Coenzyme a | C21 H36 N7 O16 P3 S | 1 |
Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A. Lin, Y., Fletcher, C.M., Zhou, J. et al. Nature (1999) 400:86-89. DOI 10.1038/21922 · 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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