1QSR: Tetrahymena GCN5 with bound acetyl-coenzyme a

Crystal structure of tetrahymena GCN5 with bound acetyl-coenzyme a. Determined by X-ray diffraction at 2.0 Å resolution. Released 8 Sept 1999.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Tetrahymena thermophila
Chains
1
Atoms
1,483
Mol. weight
20.15 kDa
Ligands
ACO
Released
8 Sept 1999

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

Secondary structure: helices and β-sheets

1QSR 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

ElementResiduesLengthSheet
β-strand50-5451
α-helix551
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-helix166-1716
β-strand17511
α-helix182-1854
β-strand18612
β-strand18912
β-strand196-20161

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
TGCN5 histone acetyl transferaseAprotein162Tetrahymena thermophilaQ27198 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1QSR_1 TGCN5 HISTONE ACETYL TRANSFERASE (chains A)
LDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQKVIG
GICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNFAIGY
FKKQGFTKEHRMPQEKWKGYIKDYDGGTLMECYIHPYVDYGR

Ligands and cofactors

IDNameFormulaCopies
ACOAcetyl coenzyme *aC23 H38 N7 O17 P3 S1

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:

Browse structure collections

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