5GCN: Histone acetyltransferase GCN5

Catalytic domain of tetrahymena GCN5 histone acetyltransferase in complex with coenzyme a. Determined by solution NMR. Released 19 Jul 1999.

Method
Solution NMR
Organism
Tetrahymena thermophila
Chains
1
Atoms
1,435
Mol. weight
20.5 kDa
Ligands
COA
Released
19 Jul 1999

Explore 5GCN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5GCN contains 6 α-helices and 11 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, 11 β-strands

ElementResiduesLengthSheet
β-strand6-1051
α-helix17-3216
α-helix38-458
β-strand51-5661
β-strand62-7091
β-strand7612
β-strand77-8261
α-helix86-883
α-helix94-10714
β-strand11212
β-strand115-11623
α-helix119-12810
β-strand13114
α-helix138-1414
β-strand153-15423
β-strand15514
β-strand15712

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone acetyltransferase GCN5Aprotein166Tetrahymena thermophilaQ27198 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5GCN_1 HISTONE ACETYLTRANSFERASE GCN5 (chains A)
MKGLLDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQ
KVIGGICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNF
AIGYFKKQGFTKEHRMPQEKWKGYIKDYDGGTLMECYIHPYVDYGN

Ligands and cofactors

IDNameFormulaCopies
COACoenzyme aC21 H36 N7 O16 P3 S1

Primary citation

Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A. Lin, Y., Fletcher, C.M., Zhou, J. et al. Nature (1999) 400:86-89. DOI 10.1038/21922 · 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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