1Q2C: Histone acetyltransferase GCN5

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.

Method
X-ray diffraction
Resolution
2.25 Å
Organism
Tetrahymena thermophila
Chains
2
Atoms
1,503
Mol. weight
21.98 kDa
Ligands
COA
Released
3 Aug 2004

Explore 1Q2C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand50-5451
α-helix60-7617
α-helix82-909
β-strand94-10181
β-strand105-115111
β-strand120-12891
α-helix130-1323
α-helix137-15115
β-strand156-16161
α-helix164-1718
β-strand17511
α-helix182-1843
β-strand196-20161

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
histone acetyltransferase GCN5Aprotein162Tetrahymena thermophilaQ27198 (AlphaFold model)
Histone H4 peptideBprotein19
Sequence of entity 1 (A), FASTA
>1Q2C_1 histone acetyltransferase GCN5 (chains A)
LDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQKVIG
GICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNFAIGY
FKKQGFTKEHRMPQEKWKGYIKDYDGGTLMECYIHPYVDYGR
Sequence of entity 2 (B), FASTA
>1Q2C_2 Histone H4 peptide (chains B)
SGRGKGGKGLGKGGAKRHR

Ligands and cofactors

IDNameFormulaCopies
COACoenzyme aC21 H36 N7 O16 P3 S1

Primary citation

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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