3QM0: RTT109-AC-CoA complex

Name: PDB 3QM0: Crystal structure of RTT109-AC-CoA complex
Published: 2011-02-16
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Crystal structure of RTT109-AC-CoA complex. Determined by X-ray diffraction at 3.1 Å resolution. Released 16 Feb 2011.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 2,973
Mol. weight: 45.86 kDa
Ligands: ACO, HG
Released: 16 Feb 2011

Explore 3QM0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3QM0 contains 13 α-helices and 19 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: 13 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	3-8	6
β-strand	12	1	1
β-strand	16-23	8	2
α-helix	24-26	3
β-strand	27-29	3	2
β-strand	45-57	13	2
β-strand	61-73	13	2
β-strand	79-90	12	2
α-helix	100-112	13
β-strand	114	1	3
α-helix	117-122	6
α-helix	182-184	3
β-strand	186-193	8	2
α-helix	215-233	19
β-strand	234	1	4
β-strand	239-243	5	2
α-helix	249-256	8
β-strand	264-266	3	2
β-strand	277	1	5
α-helix	278-280	3
α-helix	289-299	11
β-strand	307	1	5
α-helix	308-316	9
β-strand	328-334	7	2
β-strand	336	1	4
β-strand	342	1	3
β-strand	350	1	2
α-helix	355-366	12
α-helix	373-390	18
α-helix	394-395	2
β-strand	396-399	4	2
β-strand	402	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase RTT109	A	protein	388	Saccharomyces cerevisiae	Q07794 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3QM0_1 Histone acetyltransferase RTT109 (chains A)
GSMSLNDFLSSVLPVSEQFEYLSLQSIPLETHAVVTPNKDDKRVPKSTIKTQHFFSLFHQ
GKVFFSLEVYVYVTLWDEADAERLIFVSKADTNGYCNTRVSVRDITKIILEFILSIDPNY
YLQKVKPAIRSTCPREILTKICLFTRPASQYLFPDSSKNSKKHILNGEELMKWWGFILDR
LLIECFQNDTQAKLRIPGEDPARVRSYLRGMKYPLWQVGDIFTSKENSLAVYNIPLFPDD
PKARFIHQLAEEDRLLKVSLSSFWIELQERQEFKLSVTSSVMGISGYSLATPSLFPSSAD
VIVPKSRKQFRAIKKYITGEEYDTEEGAIEAFTNIRDFLLLRMATNLQSLTGKREHRERN
QPVPASNINTLAITMLKPRKKAKALPKT

Ligands and cofactors

ID	Name	Formula	Copies
ACO	Acetyl coenzyme *a	C23 H38 N7 O17 P3 S	1
HG	Mercury (II) ion	Hg	2

Primary citation

Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. Tang, Y., Holbert, M.A., Wurtele, H. et al. Nat Struct Mol Biol (2008) 15:738-745. DOI 10.1038/nsmb.1448 · PubMed

Other PDB entries of the same protein (UniProt Q07794 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2ZFN 1.9 Å, Self-acetylation mediated histone H3 lysine 56 acetylation by rtt109
3CZ7 2.0 Å, Molecular Basis for the Autoregulation of the Protein Acetyl Transferase Rtt109
2RIM 2.2 Å, Crystal structure of Rtt109
3Q66 2.71 Å, Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex…
3Q68 2.71 Å, Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex…
3Q33 2.8 Å, Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated…
3Q35 3.3 Å, Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated…
6F0Y Rtt109 peptide bound to Asf1
6O22 Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex…

Browse structure collections

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