1Q2D: Histone acetyltransferase GCN5

Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue p53 peptide. Determined by X-ray diffraction at 2.25 Å resolution. Released 3 Aug 2004.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: Tetrahymena thermophila
Chains: 2
Atoms: 1,498
Mol. weight: 22.24 kDa
Ligands: COA
Released: 3 Aug 2004

Explore 1Q2D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Q2D contains 6 α-helices and 9 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.

Chain A: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	50-54	5	1
α-helix	60-76	17
α-helix	82-89	8
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	182-185	4
β-strand	186	1	2
β-strand	189	1	2
β-strand	196-201	6	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
histone acetyltransferase GCN5	A	protein	162	Tetrahymena thermophila	Q27198 (AlphaFold model)
19-mer peptide fragment from p53 Tumor Suppressor	B	protein	19

Sequence of entity 1 (A), FASTA

>1Q2D_1 histone acetyltransferase GCN5 (chains A)
LDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQKVIG
GICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNFAIGY
FKKQGFTKEHRMPQEKWKGYIKDYDGGTLMECYIHPYVDYGR

Sequence of entity 2 (B), FASTA

>1Q2D_2 19-mer peptide fragment from p53 Tumor Suppressor (chains B)
NTSSSPQPKKKPLDGEYFT

Ligands and cofactors

ID	Name	Formula	Copies
COA	Coenzyme a	C21 H36 N7 O16 P3 S	1

Primary citation

Molecular basis for GCN5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates. Poux, A.N., Marmorstein, R. Biochemistry (2003) 42:14366-14374. DOI 10.1021/bi035632n · PubMed

Other PDB entries of the same protein (UniProt Q27198 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1QST 1.7 Å, Crystal structure of tetrahymena GCN5
1QSR 2.0 Å, Crystal structure of tetrahymena GCN5 with bound acetyl-coenzyme a
1M1D 2.2 Å, Tetrahymena GCN5 with bound bisubstrate analog inhibitor
1QSN 2.2 Å, Crystal structure of tetrahymena GCN5 with bound coenzyme a and histone H3 peptide
1Q2C 2.25 Å, Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4…
1PU9 2.3 Å, Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3…
1PUA 2.3 Å, Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a Phosphorylated,…
5GCN Catalytic domain of tetrahymena GCN5 histone acetyltransferase in complex with coenzyme a

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