1MJA: Yeast Esa1 histone acetyltransferase domain

Name: PDB 1MJA: Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A
Published: 2002-10-30
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A. Determined by X-ray diffraction at 2.26 Å resolution. Released 30 Oct 2002.

Method: X-ray diffraction
Resolution: 2.26 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 2,491
Mol. weight: 34.18 kDa
Ligands: COA
Released: 30 Oct 2002

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

Secondary structure: helices and β-sheets

1MJA contains 12 α-helices and 17 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: 12 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	169-172	4	1
β-strand	175-177	3	1
α-helix	178-179	2
β-strand	194-197	4	1
β-strand	204-205	2	1
α-helix	208-215	8
β-strand	226-230	5	2
β-strand	234-240	7	2
α-helix	241-243	3
α-helix	245-256	12
β-strand	271-280	10	2
β-strand	283-293	11	2
β-strand	300-302	3	3
β-strand	305-307	3	2
α-helix	309-311	3
α-helix	316-330	15
β-strand	335	1	4
β-strand	336-337	2	3
α-helix	341-342	2
α-helix	343-363	21
β-strand	367-369	3	5
α-helix	370-377	8
β-strand	379	1	4
α-helix	381-391	11
β-strand	394-397	4	5
β-strand	400-404	5	5
α-helix	407-418	12
α-helix	426-428	3
β-strand	429	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Esa1 protein	A	protein	278	Saccharomyces cerevisiae	Q08649 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1MJA_1 Esa1 protein (chains A)
MKEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKK
CTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMT
RRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSP
EKPLSDLGLLSYRAYWSDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYY
KGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKPPV

Ligands and cofactors

ID	Name	Formula	Copies
COA	Coenzyme a	C21 H36 N7 O16 P3 S	1

Primary citation

The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate. Yan, Y., Harper, S., Speicher, D.W. et al. Nat Struct Biol (2002) 9:862-869. DOI 10.1038/nsb0902-638 · PubMed

Other PDB entries of the same protein (UniProt Q08649 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3TO7 1.9 Å, Crystal structure of yeast Esa1 HAT domain bound to coenzyme A with active site lysine…
1FY7 2.0 Å, Crystal structure of yeast ESA1 histone acetyltransferase domain complexed with coenzyme a
3TO9 2.0 Å, Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site…
3TO6 2.1 Å, Crystal structure of yeast Esa1 HAT domain complexed with H4K16CoA bisubstrate inhibitor
1MJ9 2.5 Å, Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A
1MJB 2.5 Å, Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with…
5J9T 2.7 Å, Crystal structure of the NuA4 core complex
5J9W 2.8 Å, Crystal structure of the NuA4 core complex
5J9U 2.95 Å, Crystal structure of the NuA4 core complex
5J9Q 3.25 Å, Crystal structure of the NuA4 core complex
7VVU 3.4 Å, NuA4 HAT module bound to the nucleosome
8X2X 3.8 Å, The piccolo NuA4 bound to the H2A.Z nucleosome complex at pre-H4-acetylation state

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