1M1D: TGCN5 histone acetyl transferase

Name: PDB 1M1D: Tetrahymena GCN5 with bound bisubstrate analog inhibitor
Published: 2002-10-30
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Tetrahymena GCN5 with bound bisubstrate analog inhibitor. Determined by X-ray diffraction at 2.2 Å resolution. Released 30 Oct 2002.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Tetrahymena thermophila
Chains: 4
Atoms: 2,965
Mol. weight: 44.94 kDa
Released: 30 Oct 2002

Explore 1M1D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M1D contains 12 α-helices and 14 β-strands across 2 chains. 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, 7 β-strands

Element	Residues	Length	Sheet
β-strand	49-55	7	1
α-helix	60-76	17
α-helix	82-89	8
β-strand	94-101	8	1
β-strand	105-115	11	1
β-strand	120-128	9	1
α-helix	130-132	3
α-helix	137-151	15
β-strand	156-162	7	1
α-helix	166-170	5
β-strand	175	1	1
α-helix	182-184	3
α-helix	190-192	3
β-strand	195-201	7	1

Chain C: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	350-355	6	2
α-helix	360-376	17
α-helix	382-389	8
β-strand	394-401	8	2
β-strand	405-415	11	2
β-strand	420-428	9	2
α-helix	430-432	3
α-helix	437-451	15
β-strand	456-461	6	2
α-helix	466-471	6
β-strand	475	1	2
β-strand	496-501	6	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
TGCN5 histone acetyl transferase	A, C	protein	163	Tetrahymena thermophila	Q27198 (AlphaFold model)
Histone H3	B, D	protein	20		P61830 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1M1D_1 TGCN5 HISTONE ACETYL TRANSFERASE (chains A, C)
LLDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQKVI
GGICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNFAIG
YFKKQGFTKEHRMPQEKWKGYIKDYDGGTLMECYIHPYVDYGR

Sequence of entity 2 (B, D), FASTA

>1M1D_2 HISTONE H3 (chains B, D)
ARTKQTARKSTGGKAPRKQL

Primary citation

Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor. Poux, A.N., Cebrat, M., Kim, C.M. et al. Proc Natl Acad Sci U S A (2002) 99:14065-14070. DOI 10.1073/pnas.222373899 · 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
1QSN 2.2 Å, Crystal structure of tetrahymena GCN5 with bound coenzyme a and histone H3 peptide
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

Browse structure collections

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