SAXSdb — 5j9t

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone acetyltransferase ESA1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain E； UniProt 141–445	Fragment：UNP residues 141-445 Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	Chromatin modification-related protein EAF6 × 1 （P47128） Enhancer of polycomb-like protein 1 × 1 （P43572） Chromatin modification-related protein YNG2 × 1 （P38806）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 141–445	Fragment：UNP residues 141-445 Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	Chromatin modification-related protein EAF6 × 1 （P47128） Enhancer of polycomb-like protein 1 × 1 （P43572） Chromatin modification-related protein YNG2 × 1 （P38806）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
3	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain I； UniProt 141–445	Fragment：UNP residues 141-445 Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	Chromatin modification-related protein EAF6 × 1 （P47128） Enhancer of polycomb-like protein 1 × 1 （P43572） Chromatin modification-related protein YNG2 × 1 （P38806）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 5J9T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1FY7 CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A Deposited 2000-09-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 160–435（276 aa） Fragment：ACETYLTRANSFERASE DOMAIN	Not recorded	NA SODIUM ION × 1 COA COENZYME A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；amonium phosphate, cacodylate,, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K	Resolution 2.00 Å R-free 0.236
1FY7 CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A Deposited 2000-09-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 160–435（276 aa） Fragment：ACETYLTRANSFERASE DOMAIN	Not recorded	NA SODIUM ION × 3 COA COENZYME A × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；amonium phosphate, cacodylate,, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K	Resolution 2.00 Å R-free 0.236
1FY7 CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A Deposited 2000-09-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 160–435（276 aa） Fragment：ACETYLTRANSFERASE DOMAIN	Not recorded	NA SODIUM ION × 6 COA COENZYME A × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；amonium phosphate, cacodylate,, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K	Resolution 2.00 Å R-free 0.236
1MJ9 Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A Deposited 2002-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 160–435（276 aa） Fragment：HISTONE ACETYLTRANSFERASE DOMAIN (Residues 160-445)	Mutation：C304S	NA SODIUM ION × 1 COA COENZYME A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.255
1MJ9 Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A Deposited 2002-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 160–435（276 aa） Fragment：HISTONE ACETYLTRANSFERASE DOMAIN (Residues 160-445)	Mutation：C304S	NA SODIUM ION × 3 COA COENZYME A × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.255
1MJ9 Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A Deposited 2002-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 160–435（276 aa） Fragment：HISTONE ACETYLTRANSFERASE DOMAIN (Residues 160-445)	Mutation：C304S	NA SODIUM ION × 6 COA COENZYME A × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.255
1MJA Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A Deposited 2002-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 160–435（276 aa） Fragment：Histone acetyltransferase domain (Residues 160-445)	Non-standard monomer：Yes (specific site not provided by mmCIF)	COA COENZYME A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.26 Å R-free 0.224
1MJA Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A Deposited 2002-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 160–435（276 aa） Fragment：Histone acetyltransferase domain (Residues 160-445)	Non-standard monomer：Yes (specific site not provided by mmCIF)	COA COENZYME A × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.26 Å R-free 0.224
1MJA Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A Deposited 2002-08-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 160–435（276 aa） Fragment：Histone acetyltransferase domain (Residues 160-445)	Non-standard monomer：Yes (specific site not provided by mmCIF)	COA COENZYME A × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.26 Å R-free 0.224
1MJB Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A Deposited 2002-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 160–435（276 aa） Fragment：Histone acetyltransferase domain (Residues 160-445)	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.234
1MJB Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A Deposited 2002-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 160–435（276 aa） Fragment：Histone acetyltransferase domain (Residues 160-445)	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	ACO ACETYL COENZYME *A × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.234
1MJB Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A Deposited 2002-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 160–435（276 aa） Fragment：Histone acetyltransferase domain (Residues 160-445)	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	ACO ACETYL COENZYME *A × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.234
2RNZ Solution structure of the presumed chromodomain of the yeast histone acetyltransferase, Esa1 Deposited 2008-03-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 17–89（73 aa） Fragment：Residues 17-89	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；295 K；Pressure AMBIENT NMR sample composition 0.1mM CHROMODOMAIN [U-99% 13C; U-99% 15N], 200mM potassium phosphate, 5mM D-DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.1mM CHROMODOMAIN [U-99% 13C; U-99% 15N], 200mM potassium phosphate, 5mM D-DTT, 100% D2O \| 100% D2O	Resolution not provided
2RO0 Solution structure of the knotted tudor domain of the yeast histone acetyltransferase, Esa1 Deposited 2008-03-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–89（89 aa） Fragment：Residues 1-89	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；295 K；Pressure AMBIENT NMR sample composition 0.35mM CHROMODOMAIN [U-99% 13C; U-99% 15N], 200mM potassium phosphate, 5mM D-DTT, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.35mM CHROMODOMAIN [U-99% 13C; U-99% 15N], 200mM potassium phosphate, 5mM D-DTT, 100% D2O \| 100% D2O	Resolution not provided
3TO6 Crystal structure of yeast Esa1 HAT domain complexed with H4K16CoA bisubstrate inhibitor Deposited 2011-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 160–435（276 aa） Fragment：UNP residues 160-435	Non-standard monomer：Yes (specific site not provided by mmCIF)	CMC CARBOXYMETHYL COENZYME *A × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M sodium cacodylate, 1.6 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.10 Å R-free 0.232
3TO7 Crystal structure of yeast Esa1 HAT domain bound to coenzyme A with active site lysine acetylated Deposited 2011-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 160–435（276 aa） Fragment：UNP residues 160-435	Non-standard monomer：Yes (specific site not provided by mmCIF)	COA COENZYME A × 1 CAD CACODYLIC ACID × 1 GOL GLYCEROL × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M sodium cacodylate, 1.6 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.90 Å R-free 0.226
3TO7 Crystal structure of yeast Esa1 HAT domain bound to coenzyme A with active site lysine acetylated Deposited 2011-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 160–435（276 aa） Fragment：UNP residues 160-435	Non-standard monomer：Yes (specific site not provided by mmCIF)	COA COENZYME A × 3 CAD CACODYLIC ACID × 3 GOL GLYCEROL × 6 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M sodium cacodylate, 1.6 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.90 Å R-free 0.226
3TO9 Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site lysine acetylated Deposited 2011-09-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 160–435（276 aa） Fragment：UNP residues 160-435	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	COA COENZYME A × 1 EDO 1,2-ETHANEDIOL × 3 SO4 SULFATE ION × 2 CAD CACODYLIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M sodium cacodylate, 1.6 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.00 Å R-free 0.234
3TO9 Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site lysine acetylated Deposited 2011-09-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 160–435（276 aa） Fragment：UNP residues 160-435	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	COA COENZYME A × 3 EDO 1,2-ETHANEDIOL × 9 SO4 SULFATE ION × 6 CAD CACODYLIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1 M sodium cacodylate, 1.6 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.00 Å R-free 0.234
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 141–445（305 aa） Fragment：UNP residues 141-445	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 141–445（305 aa） Fragment：UNP residues 141-445	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain I 141–445（305 aa） Fragment：UNP residues 141-445	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 141–445（305 aa） Fragment：UNP residues 141-445)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 141–445（305 aa） Fragment：UNP residues 141-445)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain I 141–445（305 aa） Fragment：UNP residues 141-445)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 141–445（305 aa） Fragment：UNP residues 141-445	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 141–445（305 aa） Fragment：UNP residues 141-445	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain I 141–445（305 aa） Fragment：UNP residues 141-445	Mutation：E338Q Non-standard monomer：Yes (specific site not provided by mmCIF)	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
7VVZ NuA4 bound to the nucleosome Deposited 2021-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 19 PDB declaration: 21-meric	Chain P 1–445（445 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME A × 1 MG MAGNESIUM ION × 2 ATP* ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 8.80 Å

13 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ESA1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–305； UniProt 141–445 Author chain E； PDBConstruct 1–305； UniProt 141–445 Author chain I； PDBConstruct 1–305； UniProt 141–445

Chromatin modification-related protein EAF6

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P47128

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain F； UniProt 1–113	Not recorded	Histone acetyltransferase ESA1 × 1 （Q08649） Enhancer of polycomb-like protein 1 × 1 （P43572） Chromatin modification-related protein YNG2 × 1 （P38806）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 1–113	Not recorded	Histone acetyltransferase ESA1 × 1 （Q08649） Enhancer of polycomb-like protein 1 × 1 （P43572） Chromatin modification-related protein YNG2 × 1 （P38806）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
3	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain J； UniProt 1–113	Not recorded	Histone acetyltransferase ESA1 × 1 （Q08649） Enhancer of polycomb-like protein 1 × 1 （P43572） Chromatin modification-related protein YNG2 × 1 （P38806）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 5J9T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain F 1–113（113 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–113（113 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain J 1–113（113 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain F 1–113（113 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–113（113 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain J 1–113（113 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain F 1–113（113 aa）	Not recorded	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–113（113 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain J 1–113（113 aa）	Not recorded	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
7VVZ NuA4 bound to the nucleosome Deposited 2021-11-09	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 19 PDB declaration: 21-meric	Chain Y 1–113（113 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME A × 1 MG MAGNESIUM ION × 2 ATP* ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 8.80 Å
9UUO The NuA3 histone acetyltransferase complex Deposited 2025-05-07	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain F 1–113（113 aa）	Not recorded	ZN ZINC ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.68 Å
9UUS The NuA3 histone acetyltransferase complex bound to acetyl-CoA and H3 tail Deposited 2025-05-08	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–113（113 aa）	Not recorded	ZN ZINC ION × 5 ACO ACETYL COENZYME *A × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9VKW Cryo-EM structure of the NuA3 complex bound to Ace-coenzyme A Deposited 2025-06-24	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain D 1–113（113 aa）	Not recorded	ZN ZINC ION × 4 ACO ACETYL COENZYME *A × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.13 Å

7 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	EAF6_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–113； UniProt 1–113 Author chain F； PDBConstruct 1–113； UniProt 1–113 Author chain J； PDBConstruct 1–113； UniProt 1–113

Enhancer of polycomb-like protein 1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P43572

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain G； UniProt 121–400	Fragment：UNP residues 50-400	Histone acetyltransferase ESA1 × 1 （Q08649） Chromatin modification-related protein EAF6 × 1 （P47128） Chromatin modification-related protein YNG2 × 1 （P38806）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 121–400	Fragment：UNP residues 50-400	Histone acetyltransferase ESA1 × 1 （Q08649） Chromatin modification-related protein EAF6 × 1 （P47128） Chromatin modification-related protein YNG2 × 1 （P38806）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
3	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain K； UniProt 121–400	Fragment：UNP residues 50-400	Histone acetyltransferase ESA1 × 1 （Q08649） Chromatin modification-related protein EAF6 × 1 （P47128） Chromatin modification-related protein YNG2 × 1 （P38806）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 5J9T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain G 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain N 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain N 50–400（351 aa） Fragment：UNP residues 50-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 121–400（280 aa） Fragment：UNP residues 121-400	Not recorded	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 121–400（280 aa） Fragment：UNP residues 121-400	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain K 121–400（280 aa） Fragment：UNP residues 121-400	Not recorded	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
7VVU NuA4 HAT module bound to the nucleosome Deposited 2021-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 13 PDB declaration: pentadecameric	Chain T 1–832（832 aa） Chain X 1–832（832 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME *A × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.40 Å
7VVY TRA module of NuA4 Deposited 2021-11-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain H 1–832（832 aa）	Not recorded	MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.10 Å
7VVZ NuA4 bound to the nucleosome Deposited 2021-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 19 PDB declaration: 21-meric	Chain H 1–832（832 aa） Chain T 1–832（832 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME A × 1 MG MAGNESIUM ION × 2 ATP* ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 8.80 Å
7YFN Core module of the NuA4 complex in S. cerevisiae Deposited 2022-07-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain F 1–832（832 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
7YFP The NuA4 histone acetyltransferase complex from S. cerevisiae Deposited 2022-07-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain F 1–832（832 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å
8ESC Structure of the Yeast NuA4 Histone Acetyltransferase Complex Deposited 2022-10-13	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 1–832（832 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å

9 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	EPL1_YEAST
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–280； UniProt 121–400 Author chain G； PDBConstruct 1–280； UniProt 121–400 Author chain K； PDBConstruct 1–280； UniProt 121–400

Chromatin modification-related protein YNG2

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P38806

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain H； UniProt 1–120	Fragment：UNP residues 1-120	Histone acetyltransferase ESA1 × 1 （Q08649） Chromatin modification-related protein EAF6 × 1 （P47128） Enhancer of polycomb-like protein 1 × 1 （P43572）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain D； UniProt 1–120	Fragment：UNP residues 1-120	Histone acetyltransferase ESA1 × 1 （Q08649） Chromatin modification-related protein EAF6 × 1 （P47128） Enhancer of polycomb-like protein 1 × 1 （P43572）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219
3	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain L； UniProt 1–120	Fragment：UNP residues 1-120	Histone acetyltransferase ESA1 × 1 （Q08649） Chromatin modification-related protein EAF6 × 1 （P47128） Enhancer of polycomb-like protein 1 × 1 （P43572）	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；289 K；100mM HEPES (pH 7.5), 6% 1,6-Hexanediol, 7% PEG 8000, 5% ethylene glycol, 10mM DTT.	Resolution 2.70 Å R-free 0.219

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 5J9T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2MUM Solution structure of the PHD domain of Yeast YNG2 Deposited 2014-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 222–271（50 aa） Fragment：PHD-type domain residues 222-271	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 300；Pressure ambient NMR sample composition 0.5 mM [U-13C; U-15N] protein, 300 mM sodium chloride, 2.7 mM potassium chloride, 2 mM potassium phosphate, 10 mM sodium phosphate, 0.05 mM CHAPS, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain H 1–120（120 aa） Fragment：UNP residues 1-120	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain D 1–120（120 aa） Fragment：UNP residues 1-120	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9Q Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain K 1–120（120 aa） Fragment：UNP residues 1-120	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 3.25 Å R-free 0.273
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 1–120（120 aa） Fragment：UNP residues 1-120	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1–120（120 aa） Fragment：UNP residues 1-120	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain K 1–120（120 aa） Fragment：UNP residues 1-120	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；298 K；100mM NaCitrate (pH 6.5), 1.79M ammonium sulfate, 5%(w/v) glycerol	Resolution 2.95 Å R-free 0.246
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 1–120（120 aa） Fragment：UNP residues 1-120	Not recorded	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 1–120（120 aa） Fragment：UNP residues 1-120	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
5J9W Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain L 1–120（120 aa） Fragment：UNP residues 1-120	Not recorded	ACO ACETYL COENZYME *A × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；100 mM HEPES (pH 7.5), 9% PEG 20000, 8% glycerol, 7% 2-Propanol, 10% 1,6-Hexanediol, 10 mM DTT	Resolution 2.80 Å R-free 0.271
7VVU NuA4 HAT module bound to the nucleosome Deposited 2021-11-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 13 PDB declaration: pentadecameric	Chain V 1–282（282 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME *A × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.40 Å
7VVZ NuA4 bound to the nucleosome Deposited 2021-11-09	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 19 PDB declaration: 21-meric	Chain V 1–282（282 aa）	Not recorded	CMC CARBOXYMETHYL COENZYME A × 1 MG MAGNESIUM ION × 2 ATP* ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 8.80 Å

6 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	YNG2_YEAST
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain D； PDBConstruct 1–120； UniProt 1–120 Author chain H； PDBConstruct 1–120； UniProt 1–120 Author chain L； PDBConstruct 1–120； UniProt 1–120

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	5j9t
Deposition date deposition_date	2016-04-11
Structure title title	Crystal structure of the NuA4 core complex
Keywords keywords	NuA4, nucleosome, histone, acetylation, TRANSFERASE; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	52.51 Å
Radius of gyration Rg (electron density) rg_electron	52.47 Å
Forward intensity I(0) i0	984178000.00
Molecular weight molecular_weight	263470.0 kDa
Excluded volume excluded_volume	330500 Å³
Envelope volume envelope_volume	514370 Å³
Hydration-shell volume shell_volume	81573 Å³
Envelope diameter envelope_diameter	174.7 Å
Shell Rg shell_rg	56.64 Å
Envelope Rg envelope_rg	50.85 Å
Shape Rg shape_rg	52.47 Å
Total Rg total_rg	52.62 Å
Total atoms total_atoms	18581
Residues n_residues	2217
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	176.7 Å
Rg (real space) rg_real	52.44 Å
Rg uncertainty (real space) rg_real_error	1.83 Å
I(0) (real space) i0_real	9.8420e+08
I(0) uncertainty (real space) i0_real_error	1.8540e+07
Rg (reciprocal space) rg_reciprocal	52.55 Å
I(0) (reciprocal space) i0_reciprocal	984300000.0000
Solution quality estimate total_estimate	0.8940
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	64.8 Å
Skewness Skewness skewness	0.167
Kurtosis Kurtosis kurtosis	-0.655
Angular range angular_range	— – 0.1500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	81460000.0000
Real-space data points n_real_points	31
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.904

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Histone acetyltransferase ESA1
Molecular weight formula_weight	36556.9 kDa
EC 编号 ec_number	2.3.1.48
Mutation mutation	E338Q
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,A,I
Atom count atom_count	18881

HEDEIKKLRTSGSMTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPQKPLSDLGLLSYRAYWSDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKPPVFTASQLRFAW

来源 Source

来源生物 organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
通用名 common_name	;Baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Chromatin modification-related protein EAF6
Molecular weight formula_weight	12915.7 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,B,J

MTDELKSYEALKAELKKSLQDRREQEDTFDNLQQEIYDKETEYFSHNSNNNHSGHGGAHGSKSHYSGNIIKGFDTFSKSHHSHADSAFNNNDRIFSLSSATYVKQQHGQSQND

来源 Source

来源生物 organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
通用名 common_name	;Baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Enhancer of polycomb-like protein 1
Molecular weight formula_weight	33320.5 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,C,K

IPTPDASMTWNEYDKFYTGSFQETTSYIKFSATVEDCCGTNYNMDERDETFLNEQVNKGSSDILTEDEFEILCSSFEHAIHERQPFLSMDPESILSFEELKPTLIKSDMADFNLRNQLNHEINSHKTHFITQFDPVSQMNTRPLIQLIEKFGSKIYDYWRERKIEVNGYEIFPQLKFERPGEKEEIDPYVCFRRREVRHPRKTRRIDILNSQRLRALHQELKNAKDLALLVAKRENVSLNWINDELKIFDQRVKIKNLKRSLNISGEDDDLINHKRKRPT

来源 Source

来源生物 organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
通用名 common_name	;Baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	Chromatin modification-related protein YNG2
Molecular weight formula_weight	13828.9 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,D,L

MDPSLVLEQTIQDVSNLPSEFRYLLEEIGSNDLKLIEEKKKYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQSLQREKCVLANTALFLIARHLNKLEKNIALLEEDGVLAPV

来源 Source

来源生物 organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
通用名 common_name	;Baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Escherichia coli

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	300

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d5j9ta_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamily	d.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family family	d.108.1.1 — N-acetyl transferase, NAT

Domain ID domain_id	d5j9te_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamily	d.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family family	d.108.1.1 — N-acetyl transferase, NAT

Domain ID domain_id	d5j9ti_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamily	d.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family family	d.108.1.1 — N-acetyl transferase, NAT

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8. Citations (1)

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Unit-cell length a length_a	86.685 Å
Unit-cell length b length_b	137.582 Å
Unit-cell length c length_c	168.076 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.63 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	29.971 Å
R factor r_factor	0.1877
R_work r_work	0.1871
R_free r_free	0.2193

fit	/app/data/saxs_computation/j9/5j9t/5j9t.fit
pddf	/app/data/pr_computation/j9/5j9t/5j9t.pr.out
profile	/app/data/saxs_computation/j9/5j9t/5j9t.dat

Crystal structure of the NuA4 core complex

1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone acetyltransferase ESA1

State in the Current Structure

Other States of the Same Protein in the Database

Chromatin modification-related protein EAF6

State in the Current Structure

Other States of the Same Protein in the Database

Enhancer of polycomb-like protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Chromatin modification-related protein YNG2

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)