SAXSdb — 2rnz

Histone acetyltransferase ESA1

Saccharomyces cerevisiae

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 17–89	Fragment：Residues 17-89	No other associated polymer	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

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 2RNZ	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 ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 method 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 method 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 ligand/ion Different experimental method 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 method 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 method 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 mutation/modification 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 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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
2RO0 Solution structure of the knotted tudor domain of the yeast histone acetyltransferase, Esa1 Deposited 2008-03-01	Different construct Different experimental conditions	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 method 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 ligand/ion Different experimental method 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 method 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 mutation/modification 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 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 construct Different mutation/modification Different oligomeric state Different experimental method 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 construct Different mutation/modification Different oligomeric state Different experimental method 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 construct Different mutation/modification Different oligomeric state Different experimental method 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
5J9T Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different mutation/modification Different oligomeric state Different experimental method 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)	No recorded non-water small molecule	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
5J9T Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different mutation/modification Different oligomeric state Different experimental method 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；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
5J9T Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different mutation/modification Different oligomeric state Different experimental method 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)	No recorded non-water small molecule	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
5J9U Crystal structure of the NuA4 core complex Deposited 2016-04-11	Different construct Different mutation/modification Different oligomeric state Different experimental method 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 oligomeric state Different experimental method 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 oligomeric state Different experimental method 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 construct Different mutation/modification Different oligomeric state Different experimental method 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 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 31 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 22–94； UniProt 17–89

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.

Entry ID entry_id	2rnz
Deposition date deposition_date	2008-03-01
Structure title title	Solution structure of the presumed chromodomain of the yeast histone acetyltransferase, Esa1
Keywords keywords	;Esa1, HAT, chromodomain, tudor domain, RNA binding, Activator, Chromatin regulator, Transcription, Transcription regulation, Transferase ;; TRANSFERASE
Experimental Method method	SOLUTION NMR

Radius of gyration Rg (Guinier) rg_guinier	17.88 Å
Radius of gyration Rg (electron density) rg_electron	17.18 Å
Forward intensity I(0) i0	741212000.00
Molecular weight molecular_weight	220650.0 kDa
Excluded volume excluded_volume	273090 Å³
Envelope volume envelope_volume	83974 Å³
Hydration-shell volume shell_volume	28124 Å³
Envelope diameter envelope_diameter	92.0 Å
Shell Rg shell_rg	32.30 Å
Envelope Rg envelope_rg	25.95 Å
Shape Rg shape_rg	17.16 Å
Total Rg total_rg	17.82 Å
Total atoms total_atoms	30640
Residues n_residues	1880
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

Maximum dimension Dmax dmax	48.2 Å
Rg (real space) rg_real	16.80 Å
Rg uncertainty (real space) rg_real_error	0.08 Å
I(0) (real space) i0_real	7.0570e+08
I(0) uncertainty (real space) i0_real_error	5.8840e+06
Rg (reciprocal space) rg_reciprocal	18.07 Å
I(0) (reciprocal space) i0_reciprocal	741200000.0000
Solution quality estimate total_estimate	0.6833
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	18.2 Å
Skewness Skewness skewness	0.365
Kurtosis Kurtosis kurtosis	-0.373
Angular range angular_range	— – 0.4450 Å⁻¹
Current regularization parameter α current_alpha	3.6410
Highest regularization parameter α highest_alpha	565200.0000
Real-space data points n_real_points	75
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.003; Oscil: 0.977; Stabil: 0.985; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

Description description	Histone acetyltransferase ESA1
Molecular weight formula_weight	11071.5 kDa
EC 编号 ec_number	2.3.1.48
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	30640

Solution structure of the presumed chromodomain of the yeast histone acetyltransferase, Esa1

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

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Escherichia coli

fit	/app/data/saxs_computation/rn/2rnz/2rnz.fit
pddf	/app/data/pr_computation/rn/2rnz/2rnz.pr.out
profile	/app/data/saxs_computation/rn/2rnz/2rnz.dat