1QSN: TGCN5 histone acetyl transferase

Name: PDB 1QSN: Crystal structure of tetrahymena GCN5 with bound coenzyme a and histone H3 peptide
Published: 1999-09-08
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Crystal structure of tetrahymena GCN5 with bound coenzyme a and histone H3 peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 8 Sept 1999.

Method: X-ray diffraction
Resolution: 2.2 Å
Organisms: Tetrahymena thermophila, Saccharomyces cerevisiae
Chains: 2
Atoms: 1,602
Mol. weight: 21.27 kDa
Ligands: COA
Released: 8 Sept 1999

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

Secondary structure: helices and β-sheets

1QSN contains 7 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: 7 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
α-helix	116-118	3
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
TGCN5 histone acetyl transferase	A	protein	162	Tetrahymena thermophila	Q27198 (AlphaFold model)
Histone H3	B	protein	11	Saccharomyces cerevisiae	P61830 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1QSN_1 TGCN5 HISTONE ACETYL TRANSFERASE (chains A)
LDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQKVIG
GICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNFAIGY
FKKQGFTKEHRMPQEKWKGYIKDYDGGTLMECYIHPYVDYGR

Sequence of entity 2 (B), FASTA

>1QSN_2 HISTONE H3 (chains B)
KSTGGKAPRKQ

Ligands and cofactors

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

Primary citation

Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Rojas, J.R., Trievel, R.C., Zhou, J. et al. Nature (1999) 401:93-98. DOI 10.1038/43487 · 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
1Q2C 2.25 Å, Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4…
1Q2D 2.25 Å, Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue p53 peptide
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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