1PUA: Hat A1

Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a Phosphorylated, 19-residue Histone H3 peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 23 Sept 2003.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Tetrahymena thermophila
Chains
2
Atoms
1,710
Mol. weight
22.32 kDa
Ligands
COA
Released
23 Sept 2003

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

Secondary structure: helices and β-sheets

1PUA 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

ElementResiduesLengthSheet
β-strand50-5451
α-helix60-7617
α-helix82-898
β-strand94-10181
β-strand105-115111
β-strand120-12891
α-helix130-1323
α-helix137-15115
β-strand156-16161
α-helix164-1718
β-strand17511
α-helix182-1854
β-strand18612
β-strand18912
β-strand196-20161

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Hat A1Aprotein163Tetrahymena thermophilaQ27198 (AlphaFold model)
Histone H3Bprotein19P61830 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1PUA_1 HAT A1 (chains A)
LLDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQKVI
GGICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNFAIG
YFKKQGFTKEHRMPQEKWKGYIKDYDGGTLMECYIHPYVDYGR
Sequence of entity 2 (B), FASTA
>1PUA_2 Histone H3 (chains B)
QTARKSTGGKAPRKQLASK

Ligands and cofactors

IDNameFormulaCopies
COACoenzyme aC21 H36 N7 O16 P3 S1

Primary citation

Structural basis for histone and phospho-histone binding by the GCN5 histone acetyltransferase. Clements, A., Poux, A.N., Lo, W.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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