6v8b

Crystal structure of the p300 acetyltransferase domain with AcCoA competitive inhibitor 1

Method: X-RAY DIFFRACTION D_max: 68.1 Å Quality: GOOD

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

Histone acetyltransferase p300

Homo sapiens

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 1287–1666	Mutation：M1652G	QRY 4-(2-{[(1R)-2-(1H-indol-3-yl)-2-oxo-1-phenylethyl]amino}ethyl)benzene-1-sulfonamide × 1 CL CHLORIDE ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；INDEX F6. 25% PEG3350, 0.2 M Ammonium sulfate, 0.1 M BisTris pH 5.5	Resolution 3.13 Å R-free 0.316

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 6V8B	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1L3E NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex Deposited 2002-02-26	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 × 2 PDB declaration: dimeric	Chain B 323–423（101 aa） Fragment：cysteine/histidine-rich 1 domain (CH1)	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 100 mM NaCl；Pressure ambient NMR sample composition 1mM CTAD/CH1 complex U-15N,13C; 0.1mM ZnSO4; 1mM DTT \| 90% D2O, 10% H2O NMR sample composition 1mM CTAD/CH1 complex U-15N,13C; 0.1mM ZnSO4; 1mM DTT \| 99.9% D2O NMR sample composition 1mM CTAD/CH1 complex U-15N; 0.1mM ZnSO4; 1mM DTT \| 90% D2O, 10% H2O NMR sample composition 1mM CTAD/CH1 complex; 0.1mM ZnSO4; 1mM DTT \| 99.9% D2O NMR sample composition 1mM CTAD/CH1 complex 10% U-13C; 0.1mM ZnSO4; 1mM DTT \| 99.9% D2O	Resolution not provided
1P4Q Solution structure of the CITED2 transactivation domain in complex with the p300 CH1 domain Deposited 2003-04-23	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 × 2 PDB declaration: dimeric	Chain B 323–423（101 aa） Fragment：cysteine/histidine-rich 1 (CH1) domain	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 100mM NaCl；Pressure ambient NMR sample composition 1mM CITED/p300;10mM deut-MES, pH 6.0; 100mM NaCl; 0.1mM ZnSO4 \| 99.9% D2O NMR sample composition 1mM CITED/p300 U-15N;10mM deut-MES, pH 6.0; 100mM NaCl; 0.1mM ZnSO4 \| 90% H2O/10% D2O NMR sample composition 1mM CITED/p300 U-15N;10mM deut-MES, pH 6.0; 100mM NaCl; 0.1mM ZnSO4 \| 99.9% D2O NMR sample composition 1mM CITED/p300 U-15N,13C;10mM deut-MES, pH 6.0; 100mM NaCl; 0.1mM ZnSO4 \| 90% H2O/10% D2O NMR sample composition 1mM CITED/p300 U-15N,13C;10mM deut-MES, pH 6.0; 100mM NaCl; 0.1mM ZnSO4 \| 99.9% D2O NMR sample composition 1mM CITED/p300 10%13C;10mM deut-MES, pH 6.0; 100mM NaCl; 0.1mM ZnSO4 \| 99.9% D2O	Resolution not provided
2K8F Structural Basis for the Regulation of p53 Function by p300 Deposited 2008-09-08	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 × 2 PDB declaration: dimeric	Chain A 1723–1812（90 aa） Fragment：UNP residues 1723-1812	Mutation：C1738A, C1746A, C1789A, C1790A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.3；308 K；Ionic strength (raw mmCIF value) 200；Pressure ambient NMR sample composition 1.1 mM TAZ2, 1.0 mM [U-100% 15N] TAD(1-39), 1.0 mM [U-100% 13C; U-100% 15N] TAD(1-39), 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.0 mM [U-100% 15N] TAZ2, 1.1 mM TAD(1-39), 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.0 mM [U-100% 13C; U-100% 15N] TAZ2, 1.1 mM TAD(1-39), 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.0 mM TAZ2, 1.1 mM TAD(1-39), 100% D2O \| 100% D2O	Resolution not provided
2MH0 Solution NMR structure of the p300 Taz2:ETAD1 complex Deposited 2013-11-12	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 × 2 PDB declaration: dimeric	Chain B 1723–1812（90 aa） Fragment：TAZ-type 2 zinc finger residues 1723-1812	Mutation：C1738A, C1746A, C1789A, C1790A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；288 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1.4 mM [U-99% 13C; U-99% 15N] ETAD1, 2 mM Taz2, 20 mM MES, 1 mM sodium azide, 5 mM beta-mercaptoethanol, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 3078 uM ETAD1, 1038 uM [U-99% 13C; U-99% 15N] Taz2, 20 mM MES, 1 mM sodium azide, 5 mM beta-mercaptoethanol, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2MZD Characterization of the p300 Taz2-p53 TAD2 Complex and Comparison with the p300 Taz2-p53 TAD1 Complex Deposited 2015-02-11	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 × 2 PDB declaration: dimeric	Chain A 1723–1812（90 aa） Fragment：UNP residues 1723-1812	Mutation：C16A, C24A, C67A, C68A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.3；308 K；Ionic strength (raw mmCIF value) 200；Pressure ambient NMR sample composition 1.1 mM Taz2 domain of Histone Acetyltransferase p300, 1.0 mM [U-100% 13C; U-100% 15N] TAD2 sub-domain of Cellular Tumor Antigen p53, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.0 mM [U-100% 15N] Taz2 domain of Histone Acetyltransferase p300, 1.1 mM TAD2 sub-domain of Cellular Tumor Antigen p53, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.0 mM [U-100% 13C; U-100% 15N] Taz2 domain of Histone Acetyltransferase p300, 1.1 mM TAD2 sub-domain of Cellular Tumor Antigen p53, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.0 mM Taz2 domain of Histone Acetyltransferase p300, 1.1 mM TAD2 sub-domain of Cellular Tumor Antigen p53, 100% D2O \| 100% D2O	Resolution not provided
3BIY Crystal structure of p300 histone acetyltransferase domain in complex with a bisubstrate inhibitor, Lys-CoA Deposited 2007-12-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1666（380 aa） Fragment：acetyltransferase domain	Mutation：K1637R, M1652G	BR BROMIDE ION × 5 01K [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R,20R)-20-carbamoyl-3-hydroxy-2,2-dimethyl-4,8,14,22-tetraoxo-12-thia-5,9,15,21-tetraazatricos-1-yl dihydrogen diphosphate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M HEPES sodium pH 7.5, 20% w/v polyethylene glycol 4,000, 10% v/v 2-Propanol , VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.70 Å R-free 0.213
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	CL CHLORIDE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 10 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain J 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 11 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain K 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 12 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain L 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	CL CHLORIDE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain G 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain H 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3I3J Crystal Structure of the Bromodomain of Human EP300 Deposited 2009-06-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 9 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain I 1040–1161（122 aa） Fragment：UNP RESIDUES 1040-1161	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.33 Å R-free 0.275
3IO2 Crystal structure of the Taz2 domain of p300 Deposited 2009-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1723–1836（114 aa） Fragment：residues 1723-1836	Mutation：C1738A, C1746A, C1789A, C1790A	ZN ZINC ION × 3 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 6.3；277 K；Protein solution: 30 mg/ml Taz2, 25 mM MES pH 6.3, 100 mM NaCl, 6% glycerol, 10% TCEP. Precipitating solution: 3.2 M AMS in MES buffer pH 6.0, 10 % ethylene glycol. Both solutions mixed 1:1 and kept under oil, Microbatch, temperature 277K	Resolution 2.50 Å R-free 0.236
3P57 Crystal structure of the p300 TAZ2 domain bound to MEF2 on DNA Deposited 2010-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 7 PDB declaration: tridecameric	Chain P 1726–1835（110 aa）	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；288 K；16% PEG 1000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 288K	Resolution 2.19 Å R-free 0.272
3T92 Crystal structure of the Taz2:C/EBPepsilon-TAD chimera protein Deposited 2011-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1723–1818（96 aa） Fragment：unp residues 1723-1818; unp residues 37-61	Mutation：C1738A, C1746A, C1789A, C1790A,	ZN ZINC ION × 3 TCE 3,3',3''-phosphanetriyltripropanoic acid × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 ACN ACETONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions Micro batch under oil；pH 8.5；277 K；200mM NaCl, 5mM TCEP and 20% isopropanol, pH 8.5, Micro batch under oil, temperature 277K	Resolution 1.50 Å R-free 0.228
4BHW Structural basis for autoinhibition of the acetyltransferase activity of p300 Deposited 2013-04-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1043–1519（477 aa） Fragment：P300 CORE, RESIDUES 1043-1519,1581-1666 Chain A 1581–1666（86 aa） Fragment：P300 CORE, RESIDUES 1043-1519,1581-1666 Chain B 1043–1519（477 aa） Fragment：P300 CORE, RESIDUES 1043-1519,1581-1666 Chain B 1581–1666（86 aa） Fragment：P300 CORE, RESIDUES 1043-1519,1581-1666	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	ZN ZINC ION × 7 01K [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R,20R)-20-carbamoyl-3-hydroxy-2,2-dimethyl-4,8,14,22-tetraoxo-12-thia-5,9,15,21-tetraazatricos-1-yl dihydrogen diphosphate × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；100 MM HEPES, PH 7.5, 20% PEG3350, 0.2M NACL	Resolution 2.80 Å R-free 0.244
4PZR Crystal structure of p300 histone acetyltransferase domain in complex with Coenzyme A Deposited 2014-03-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1664（378 aa） Fragment：acetyltransferase domain (UNP residues 1287-1664)	Mutation：Y1467F	PEG DI(HYDROXYETHYL)ETHER × 2 DMS DIMETHYL SULFOXIDE × 1 COA COENZYME A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1 M HEPES, pH 7.5, 16% PEG3350, 3-10% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.10 Å R-free 0.219
4PZS Crystal structure of p300 histone acetyltransferase domain in complex with Acetyl-Coenzyme A Deposited 2014-03-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1664（378 aa） Fragment：acetyltransferase domain (UNP residues 1287-1664)	Mutation：Y1467F	ACO ACETYL COENZYME A × 1 DMS* DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1 M HEPES, pH 7.5, 16% PEG3350, 3-10% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.94 Å R-free 0.230
4PZT Crystal structure of p300 histone acetyltransferase domain in complex with an inhibitor, Acetonyl-Coenzyme A Deposited 2014-03-31	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1664（378 aa） Fragment：acetyltransferase domain (UNP residues 1287-1664)	Mutation：Y1467F	SOP [(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL (3R)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-{[3-OXO-3-({2-[(2-OXOPROPYL)THIO]ETHYL}AMINO)PROPYL]AMINO}BUTYL DIHYDROGEN DIPHOSPHATE × 1 DMS DIMETHYL SULFOXIDE × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1 M HEPES, pH 7.5, 16% PEG3350, 3-10% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.236
5BT3 Crystal structure of EP300 bromodomain in complex with SGC-CBP30 chemical probe Deposited 2015-06-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1048–1161（114 aa） Fragment：bromodomain, UNP residues 1048-1161	Not recorded	2LO 2-[2-(3-chloro-4-methoxyphenyl)ethyl]-5-(3,5-dimethyl-1,2-oxazol-4-yl)-1-[(2S)-2-(morpholin-4-yl)propyl]-1H-benzimidazole × 1 IPA ISOPROPYL ALCOHOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；277 K；0.1 M tri-sodium citrate dihydrate pH 5.6, 20% iso-propanol, 20% PEG 4000	Resolution 1.05 Å R-free 0.178
5KJ2 The novel p300/CBP inhibitor A-485 uncovers a unique mechanism of action to target AR in castrate resistant prostate cancer Deposited 2016-06-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1666（380 aa）	Not recorded	6TF N-[(4-fluorophenyl)methyl]-2-{(1R)-5-[(methylcarbamoyl)amino]-2',4'-dioxo-2,3-dihydro-3'H-spiro[indene-1,5'-[1,3]oxazolidin]-3'-yl}-N-[(2S)-1,1,1-trifluoropropan-2-yl]acetamide × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；290 K；25% (w/v) PEG3350, 0.2M Sodium Chloride, 0.1M BIS-TRIS buffer pH5.5	Resolution 1.95 Å R-free 0.260
5LKT Crystal structure of the p300 acetyltransferase catalytic core with butyryl-coenzyme A. Deposited 2016-07-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1043–1519（477 aa） Fragment：UNP residues 1043-1519,UNP residues 1581-1666 Chain A 1581–1666（86 aa） Fragment：UNP residues 1043-1519,UNP residues 1581-1666	Mutation：Y1467F,Y1467F Mutation：Y1467F,Y1467F	ZN ZINC ION × 4 BCO Butyryl Coenzyme A × 1 GOL GLYCEROL × 3 DMS DIMETHYL SULFOXIDE × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Tris, PEG MME 2000	Resolution 2.04 Å R-free 0.204
5LKU Crystal structure of the p300 acetyltransferase catalytic core with coenzyme A. Deposited 2016-07-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1043–1519（477 aa） Chain A 1581–1666（86 aa）	Mutation：Y1467F,Y1467F Mutation：Y1467F,Y1467F	ZN ZINC ION × 4 COA COENZYME A × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Tris, PEG MME 2000	Resolution 3.50 Å R-free 0.242
5LKX Crystal structure of the p300 acetyltransferase catalytic core with propionyl-coenzyme A. Deposited 2016-07-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1043–1519（477 aa） Chain A 1581–1666（86 aa）	Mutation：Y1467F,Y1467F Mutation：Y1467F,Y1467F	ZN ZINC ION × 4 1VU propionyl Coenzyme A × 1 DMS DIMETHYL SULFOXIDE × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Tris, PEG MME 2000, DMSO	Resolution 2.52 Å R-free 0.239
5LKZ Crystal structure of the p300 acetyltransferase catalytic core with crotonyl-coenzyme A. Deposited 2016-07-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1043–1519（477 aa） Fragment：UNP residues 1043-1519,UNP residues 1581-1666,UNP residues 1043-1519,UNP residues 1581-1666 Chain A 1581–1666（86 aa） Fragment：UNP residues 1043-1519,UNP residues 1581-1666,UNP residues 1043-1519,UNP residues 1581-1666	Mutation：Y1467F,Y1467F,Y1467F,Y1467F Mutation：Y1467F,Y1467F,Y1467F,Y1467F	ZN ZINC ION × 4 COO CROTONYL COENZYME A × 1 GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Tris, PEG MME 2000	Resolution 2.50 Å R-free 0.234
5LPK Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM1 Deposited 2016-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1040–1161（122 aa） Fragment：bromodomain, UNP residues 1040-1161	Not recorded	XDM ~{N}-[(3-chlorophenyl)methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide × 1 SO4 SULFATE ION × 2 EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；PEG 3350, NaCl	Resolution 2.10 Å R-free 0.203
5LPK Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM1 Deposited 2016-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1040–1161（122 aa） Fragment：bromodomain, UNP residues 1040-1161	Not recorded	XDM ~{N}-[(3-chlorophenyl)methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide × 1 EDO 1,2-ETHANEDIOL × 6 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；PEG 3350, NaCl	Resolution 2.10 Å R-free 0.203
5LPK Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM1 Deposited 2016-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1040–1161（122 aa） Fragment：bromodomain, UNP residues 1040-1161	Not recorded	XDM ~{N}-[(3-chlorophenyl)methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide × 1 SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；PEG 3350, NaCl	Resolution 2.10 Å R-free 0.203
5LPK Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM1 Deposited 2016-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1040–1161（122 aa） Fragment：bromodomain, UNP residues 1040-1161	Not recorded	XDM ~{N}-[(3-chlorophenyl)methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide × 1 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；PEG 3350, NaCl	Resolution 2.10 Å R-free 0.203
5LPK Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM1 Deposited 2016-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 1040–1161（122 aa） Fragment：bromodomain, UNP residues 1040-1161	Not recorded	XDM ~{N}-[(3-chlorophenyl)methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide × 2 SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；PEG 3350, NaCl	Resolution 2.10 Å R-free 0.203
5LPK Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM1 Deposited 2016-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 1040–1161（122 aa） Fragment：bromodomain, UNP residues 1040-1161	Not recorded	XDM ~{N}-[(3-chlorophenyl)methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide × 1 SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；PEG 3350, NaCl	Resolution 2.10 Å R-free 0.203
5LPK Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM1 Deposited 2016-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain G 1040–1161（122 aa） Fragment：bromodomain, UNP residues 1040-1161	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；PEG 3350, NaCl	Resolution 2.10 Å R-free 0.203
5LPM Crystal structure of the bromodomain of human Ep300 bound to the inhibitor XDM3d Deposited 2016-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1048–1161（114 aa） Fragment：bromodomain, UNP residues 1048-1161	Not recorded	71Y ~{N}-[(1~{S},2~{S})-7-chloranyl-2-oxidanyl-1,2,3,4-tetrahydronaphthalen-1-yl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole -2-carboxamide × 2 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.5；277 K；NaCl, PEG 3350	Resolution 1.50 Å R-free 0.187
5LPM Crystal structure of the bromodomain of human Ep300 bound to the inhibitor XDM3d Deposited 2016-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1048–1161（114 aa） Fragment：bromodomain, UNP residues 1048-1161	Not recorded	71Y ~{N}-[(1~{S},2~{S})-7-chloranyl-2-oxidanyl-1,2,3,4-tetrahydronaphthalen-1-yl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole -2-carboxamide × 2 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.5；277 K；NaCl, PEG 3350	Resolution 1.50 Å R-free 0.187
5NU5 Crystal structure of the human bromodomain of EP300 bound to the inhibitor XDM-CBP Deposited 2017-04-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1048–1161（114 aa） Fragment：bromodomain	Not recorded	99E ~{N}-[[2,8-bis(oxidanyl)naphthalen-1-yl]methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide × 1 EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；KSCN, NaBr, PEG 6000, PEG 8000, PEG 10000	Resolution 1.60 Å R-free 0.185
5NU5 Crystal structure of the human bromodomain of EP300 bound to the inhibitor XDM-CBP Deposited 2017-04-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1048–1161（114 aa） Fragment：bromodomain	Not recorded	99E ~{N}-[[2,8-bis(oxidanyl)naphthalen-1-yl]methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；277 K；KSCN, NaBr, PEG 6000, PEG 8000, PEG 10000	Resolution 1.60 Å R-free 0.185
5XZC Cryo-EM structure of p300-p53 protein complex Deposited 2017-07-12	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 1046–1664（619 aa） Fragment：UNP residues 1046-1664	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 10.70 Å
6DS6 Crystal structure of p300 ZZ domain in complex with histone H3 peptide Deposited 2018-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1663–1713（51 aa）	Not recorded	ZN ZINC ION × 4 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M HEPES and 70% MPD (pH 7.5)	Resolution 1.95 Å R-free 0.253
6FGN Solution Structure of p300Taz2-p63TA Deposited 2018-01-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1723–1812（90 aa） Fragment：Taz2,transactivation domain	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.3；303 K；Ionic strength (raw mmCIF value) 200；Pressure AMBIENT NMR sample composition 1200 mM [U-13C; U-15N] Fusion construct of p300 Taz2 and the transactivation domain of p63, 25 mM MES, 200 mM NaCl, 0.5 mM TCEP, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
6FGS Solution structure of p300Taz2-p73TA1 Deposited 2018-01-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1723–1812（90 aa）	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.3；303 K；Ionic strength (raw mmCIF value) 50；Pressure AMBIENT NMR sample composition 700 uM [U-13C; U-15N] Fusion construct of p300 Taz2 and the transactivation domain 1 of p73, 25 mM MES, 50 mM NaCl, 0.5 mM TCEP, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
6GYR Transcription factor dimerization activates the p300 acetyltransferase Deposited 2018-07-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1046–1664（619 aa） Chain C 1046–1664（619 aa）	Mutation：Y1467F Mutation：Y1467F	ZN ZINC ION × 7 01K [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R,20R)-20-carbamoyl-3-hydroxy-2,2-dimethyl-4,8,14,22-tetraoxo-12-thia-5,9,15,21-tetraazatricos-1-yl dihydrogen diphosphate × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277 K；100 mM HEPES, pH 7.5, 18-22% polyethylene glycol 3350, 0.2 M NaCl	Resolution 3.10 Å R-free 0.265
6GYR Transcription factor dimerization activates the p300 acetyltransferase Deposited 2018-07-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1046–1664（619 aa） Chain D 1046–1664（619 aa）	Mutation：Y1467F Mutation：Y1467F	ZN ZINC ION × 7 01K [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R,20R)-20-carbamoyl-3-hydroxy-2,2-dimethyl-4,8,14,22-tetraoxo-12-thia-5,9,15,21-tetraazatricos-1-yl dihydrogen diphosphate × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277 K；100 mM HEPES, pH 7.5, 18-22% polyethylene glycol 3350, 0.2 M NaCl	Resolution 3.10 Å R-free 0.265
6GYT Transcription factor dimerization activates the p300 acetyltransferase Deposited 2018-07-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1047–1168（122 aa） Chain B 1047–1168（122 aa）	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；294 K；1.6 M Ammonium Sulfate, 100 mM Bicine, pH 9.0	Resolution 2.50 Å R-free 0.288
6K4N Cryo-EM structure of p300 Deposited 2019-05-24	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 1046–1664（619 aa） Fragment：UNP RESIDUES 1046-1664	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 9.80 Å
6PF1 Crystal structure of the p300 acetyltransferase domain with allosteric inhibitor CPI-090 and CoA Deposited 2019-06-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1513（227 aa） Chain A 1581–1663（83 aa）	Mutation：Y1467F Mutation：Y1467F	COA COENZYME A × 1 OJ7 3-[3-chloro-5-(trifluoromethyl)pyridin-2-yl]-2-methyl-1H-indole × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；277 K；0.1 M CHES pH 9.5, 30% w/v PEG 3000	Resolution 2.32 Å R-free 0.247
6PF1 Crystal structure of the p300 acetyltransferase domain with allosteric inhibitor CPI-090 and CoA Deposited 2019-06-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1287–1513（227 aa） Chain B 1581–1663（83 aa）	Mutation：Y1467F Mutation：Y1467F	COA COENZYME A × 1 OJ7 3-[3-chloro-5-(trifluoromethyl)pyridin-2-yl]-2-methyl-1H-indole × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；277 K；0.1 M CHES pH 9.5, 30% w/v PEG 3000	Resolution 2.32 Å R-free 0.247
6PGU Crystal structure of the p300 acetyltransferase domain with allosteric inhibitor CPI-076 and CoA Deposited 2019-06-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1519（233 aa） Chain A 1582–1663（82 aa）	Mutation：Y1467F, loop deletion Mutation：Y1467F, loop deletion	COA COENZYME A × 1 OK7 N-(thiophen-2-yl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277 K；20% MPD, 0.1 M Tris pH 8, 7.5% PEG-MME 5000	Resolution 1.72 Å R-free 0.206
6PGU Crystal structure of the p300 acetyltransferase domain with allosteric inhibitor CPI-076 and CoA Deposited 2019-06-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1287–1519（233 aa） Chain B 1582–1663（82 aa）	Mutation：Y1467F, loop deletion Mutation：Y1467F, loop deletion	COA COENZYME A × 1 OK7 N-(thiophen-2-yl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277 K；20% MPD, 0.1 M Tris pH 8, 7.5% PEG-MME 5000	Resolution 1.72 Å R-free 0.206
6V8K Crystal structure of the p300 acetyltransferase domain with peptide-competitive inhibitor 2 Deposited 2019-12-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1519（233 aa） Chain A 1581–1663（83 aa）	Mutation：Y1467F Mutation：Y1467F	COA COENZYME A × 1 QS4 1-(2-methyl-1H-indol-3-yl)-2-[(2R)-2-methylpiperidin-1-yl]ethan-1-one × 1 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.24 mM HAT, 0.12 mM CoA, 0.75 mM ligand. 200+150 (+20) nL sitting drops. Internal focus screen with microseeding. 17.5% MPD, 0.1 M Tris pH 8, 2.5 % PEG3350. Cryo 30% MPD, 5% PEG 3350, 1 mM ligand	Resolution 1.84 Å R-free 0.213
6V8N Crystal structure of the p300 acetyltransferase domain with AcCoA competitive inhibitor 17 Deposited 2019-12-11	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1666（380 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2 CL CHLORIDE ION × 1 QS1 (2R)-2-{[(2S)-2-(4-cyanophenyl)propyl]amino}-N-[5-(1-methyl-1H-pyrazol-4-yl)pyridin-2-yl]-2-phenylacetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；0.2 M Ammonium Sulfate, 0.1 M BisTris pH 5.5, 20% PEG 3350, streak-seed with loop	Resolution 2.30 Å R-free 0.247
6V90 Crystal structure of the p300 acetyltransferase domain with AcCoA competitive inhibitor 12 Deposited 2019-12-12	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1666（380 aa）	Mutation：M1652G	QSD (2R)-2-{[2-(4-cyanophenyl)ethyl]amino}-N-[5-(1-methyl-1H-pyrazol-4-yl)pyridin-2-yl]-2-phenylacetamide × 1 SO4 SULFATE ION × 2 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；INDEX F6. 0.1 M Bis-Tris pH 5.5, 0.2 M ammonium sulfate 25% w/v PEG 3350. The crystal was cryoprotected with MiTeGen Low Viscosity Cryo Oil	Resolution 2.04 Å R-free 0.241
7LJE Discovery of Spirohydantoins as Selective, Orally Bioavailable Inhibitors of p300/CBP Histone Acetyltransferases Deposited 2021-01-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1666（380 aa） Fragment：acetyltransferase domain (UNP residues 1287-1666)	Not recorded	Y2P 2-[4-[(3'R,4S)-3'-fluoro-1-[2-[(4-fluorophenyl)methyl-[(1S)-2,2,2-trifluoro-1-methyl-ethyl]amino]-2-oxo-ethyl]-2,5-dioxo-spiro[imidazolidine-4,1'-indane]-5'-yl]pyrazol-1-yl]-N-methyl-acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；290 K；25% PEG 3350, 0.2 M Ammonium Acetate, 0.1 M Bis-Tris HCl pH 5.5	Resolution 2.61 Å R-free 0.265
7LJE Discovery of Spirohydantoins as Selective, Orally Bioavailable Inhibitors of p300/CBP Histone Acetyltransferases Deposited 2021-01-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1287–1666（380 aa） Fragment：acetyltransferase domain (UNP residues 1287-1666)	Not recorded	Y2P 2-[4-[(3'R,4S)-3'-fluoro-1-[2-[(4-fluorophenyl)methyl-[(1S)-2,2,2-trifluoro-1-methyl-ethyl]amino]-2-oxo-ethyl]-2,5-dioxo-spiro[imidazolidine-4,1'-indane]-5'-yl]pyrazol-1-yl]-N-methyl-acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；290 K；25% PEG 3350, 0.2 M Ammonium Acetate, 0.1 M Bis-Tris HCl pH 5.5	Resolution 2.61 Å R-free 0.265
7LJE Discovery of Spirohydantoins as Selective, Orally Bioavailable Inhibitors of p300/CBP Histone Acetyltransferases Deposited 2021-01-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1287–1666（380 aa） Fragment：acetyltransferase domain (UNP residues 1287-1666)	Not recorded	Y2P 2-[4-[(3'R,4S)-3'-fluoro-1-[2-[(4-fluorophenyl)methyl-[(1S)-2,2,2-trifluoro-1-methyl-ethyl]amino]-2-oxo-ethyl]-2,5-dioxo-spiro[imidazolidine-4,1'-indane]-5'-yl]pyrazol-1-yl]-N-methyl-acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；290 K；25% PEG 3350, 0.2 M Ammonium Acetate, 0.1 M Bis-Tris HCl pH 5.5	Resolution 2.61 Å R-free 0.265
7LJE Discovery of Spirohydantoins as Selective, Orally Bioavailable Inhibitors of p300/CBP Histone Acetyltransferases Deposited 2021-01-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1287–1666（380 aa） Fragment：acetyltransferase domain (UNP residues 1287-1666)	Not recorded	Y2P 2-[4-[(3'R,4S)-3'-fluoro-1-[2-[(4-fluorophenyl)methyl-[(1S)-2,2,2-trifluoro-1-methyl-ethyl]amino]-2-oxo-ethyl]-2,5-dioxo-spiro[imidazolidine-4,1'-indane]-5'-yl]pyrazol-1-yl]-N-methyl-acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；290 K；25% PEG 3350, 0.2 M Ammonium Acetate, 0.1 M Bis-Tris HCl pH 5.5	Resolution 2.61 Å R-free 0.265
7SS8 Human P300 complexed with a proline-based inhibitor Deposited 2021-11-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1048–1519（472 aa） Chain A 1582–1664（83 aa）	Mutation：Y1467F, residues 1520-1581 replaced with SGGSG Mutation：Y1467F, residues 1520-1581 replaced with SGGSG	ZN ZINC ION × 2 EDO 1,2-ETHANEDIOL × 2 C0C 1-[1-(4-chlorophenyl)cyclopentane-1-carbonyl]-N-{[3-(methylcarbamoyl)phenyl]methyl}-D-prolinamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；277 K；20% PEG3350, 0.1 M MES pH 6.5	Resolution 2.15 Å R-free 0.230
7SSK Human P300 complexed with a glycine-based inhibitor Deposited 2021-11-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1048–1519（472 aa） Chain A 1582–1664（83 aa）	Mutation：Y1467F, residues 1520-1581 replaced with SGGSG Mutation：Y1467F, residues 1520-1581 replaced with SGGSG	ZN ZINC ION × 2 EDO 1,2-ETHANEDIOL × 1 C3I N-[2-(4-methoxyanilino)-2-oxoethyl]-N-methyl-1-phenylcyclopentane-1-carboxamide × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；277 K；20% PEG3350, 0.1 M MES pH 6.5	Resolution 2.36 Å R-free 0.235
7SZQ Human P300 complexed with an azaindazole inhibitor Deposited 2021-11-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1279–1666（388 aa）	Mutation：Y1467F	ETL 1-[1-(4-chlorophenyl)cyclopentane-1-carbonyl]-N-1H-pyrazolo[4,3-b]pyridin-5-yl-D-prolinamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 9.5；277 K；30% PEG400, 0.1 M CHES pH 9.5	Resolution 2.80 Å R-free 0.235
7UGI Bromodomain of EP300 liganded with BMS-536924 Deposited 2022-03-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1048–1161（114 aa）	Not recorded	N6I (3M)-4-{[(2S)-2-(3-chlorophenyl)-2-hydroxyethyl]amino}-3-[4-methyl-6-(morpholin-4-yl)-1H-benzimidazol-2-yl]pyridin-2(1H)-one × 1 PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL × 1 EDO 1,2-ETHANEDIOL × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；292 K；0.05M Potassium phosphate monobasic 20% w/v Polyethylene glycol 8,000	Resolution 2.00 Å R-free 0.274
7UGI Bromodomain of EP300 liganded with BMS-536924 Deposited 2022-03-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1048–1161（114 aa）	Not recorded	N6I (3M)-4-{[(2S)-2-(3-chlorophenyl)-2-hydroxyethyl]amino}-3-[4-methyl-6-(morpholin-4-yl)-1H-benzimidazol-2-yl]pyridin-2(1H)-one × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；292 K；0.05M Potassium phosphate monobasic 20% w/v Polyethylene glycol 8,000	Resolution 2.00 Å R-free 0.274
7VHY Crystal structure of EP300 HAT domain in complex with compound (+)-3 Deposited 2021-09-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1159–1519（361 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666) Chain A 1581–1666（86 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666)	Mutation：Y1467E Mutation：Y1467E	ZN ZINC ION × 3 6QI [(6R)-6-(1H-indazol-4-ylmethyl)-1,4-oxazepan-4-yl]-[1-(4-methoxyphenyl)cyclopentyl]methanone × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；15% PEG3350, 0.1 M HEPES (pH7.0)	Resolution 2.30 Å R-free 0.250
7VHY Crystal structure of EP300 HAT domain in complex with compound (+)-3 Deposited 2021-09-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1159–1519（361 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666) Chain B 1581–1666（86 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666)	Mutation：Y1467E Mutation：Y1467E	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；15% PEG3350, 0.1 M HEPES (pH7.0)	Resolution 2.30 Å R-free 0.250
7VHZ Crystal structure of EP300 HAT domain in complex with compound 7 Deposited 2021-09-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1159–1519（361 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666) Chain A 1581–1666（86 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666)	Mutation：Y1467E Mutation：Y1467E	ZN ZINC ION × 3 6TI (2R)-N-(2H-indazol-4-yl)-1-[1-(4-methoxyphenyl)cyclopentyl]carbonyl-pyrrolidine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG3350, 0.1 M HEPES (pH 7.0)	Resolution 2.00 Å R-free 0.219
7VHZ Crystal structure of EP300 HAT domain in complex with compound 7 Deposited 2021-09-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1159–1519（361 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666) Chain B 1581–1666（86 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666)	Mutation：Y1467E Mutation：Y1467E	ZN ZINC ION × 3 6TI (2R)-N-(2H-indazol-4-yl)-1-[1-(4-methoxyphenyl)cyclopentyl]carbonyl-pyrrolidine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG3350, 0.1 M HEPES (pH 7.0)	Resolution 2.00 Å R-free 0.219
7VI0 Crystal structure of EP300 HAT domain in complex with compound 11 Deposited 2021-09-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1159–1519（361 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666) Chain A 1581–1666（86 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666)	Mutation：Y1467E Mutation：Y1467E	ZN ZINC ION × 3 6YI (4S)-N-(3H-indazol-4-yl)-3-[1-(4-methoxyphenyl)cyclopentyl]carbonyl-1,1-bis(oxidanylidene)-1,3-thiazolidine-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；12% PEG3350, 0.1 M HEPES (pH 7.0)	Resolution 2.10 Å R-free 0.235
7VI0 Crystal structure of EP300 HAT domain in complex with compound 11 Deposited 2021-09-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1159–1519（361 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666) Chain B 1581–1666（86 aa） Fragment：(UNP residues 1159-1519)-linker-(UNP residues 1581-1666)	Mutation：Y1467E Mutation：Y1467E	ZN ZINC ION × 3 6YI (4S)-N-(3H-indazol-4-yl)-3-[1-(4-methoxyphenyl)cyclopentyl]carbonyl-1,1-bis(oxidanylidene)-1,3-thiazolidine-4-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；12% PEG3350, 0.1 M HEPES (pH 7.0)	Resolution 2.10 Å R-free 0.235
7W9V Cryo-EM structure of nucleosome in complex with p300 acetyltransferase catalytic core (complex I) Deposited 2021-12-10	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 × 9 PDB declaration: undecameric	Chain K 1035–1519（485 aa） Chain K 1581–1720（140 aa）	Mutation：Y1467F Mutation：Y1467F	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.95 Å
7XEZ NMR solution structures of p300 TAZ2 domain in complex with BRD4-NUT F1c domain binding motif #2 Deposited 2022-03-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1723–1812（90 aa）	Mutation：C1738A, C1746A, C1789A, C1790A	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.3；298 K；Pressure 1 NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] p300 TAZ2 domain in fusion with BRD4-NUT F1c domain binding motif #2, 200 mM sodium phosphate, 3 mM [U-100% 2H] DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] p300 TAZ2 domain in fusion with BRD4-NUT F1c domain binding motif #2, 200 mM sodium phosphate, 3 mM [U-100% 2H] DTT, 100% D2O \| 100% D2O	Resolution not provided
7XFG NMR solution structures of p300 TAZ2 domain in complex with BRD4-NUT F1c domain binding motif #1 Deposited 2022-04-01	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 × 2 PDB declaration: dimeric	Chain A 1723–1812（90 aa） Fragment：TAZ2 domain	Mutation：C1738A, C1746A, C1789A, C1790A	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.3；298 K；Ionic strength (raw mmCIF value) null；Pressure 1 NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] p300 TAZ2 domain, 1.5 mM BRD4-NUT fusion protein F1c domain binding motif #1, 200 mM sodium phosphate, 3.0 mM [U-100% 2H] DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] p300 TAZ2 domain, 1.5 mM BRD4-NUT fusion protein F1c domain binding motif #1, 200 mM sodium phosphate, 3.0 mM [U-100% 2H] DTT, 100% D2O \| 100% D2O	Resolution not provided
8E1D NMR-derived ensemble of the TAZ2 domain of p300 bound to the microphthalmia-associated transcription factor Deposited 2022-08-10	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 × 2 PDB declaration: dimeric	Chain A 1723–1812（90 aa）	Mutation：C1738A C1746A C1789A C1790A	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6；308 K；Ionic strength (raw mmCIF value) 20；Pressure 1 NMR sample composition 20 mM 2-(N-morpholino)ethanesulfonic acid (MES), 5 mM beta mercaptoethanol, 10 uM Zinc chloride, 1 mM [U-13C; U-15N] Microphthalmia-associated transcription factor, 1.2 mM TAZ2 domain of p300, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 20 mM 2-(N-morpholino)ethanesulfonic acid (MES), 5 mM beta mercaptoethanol, 10 mM Zinc chloride, 1.15 mM Microphthalmia-associated transcription factor, 0.95 mM [U-13C; U-15N] TAZ2 domain of p300, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
8FVF Bromodomain of EP300 liganded with CCS-1477 Deposited 2023-01-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1048–1161（114 aa） Fragment：bromodomain	Not recorded	JHL (6S)-1-[3,4-bis(fluoranyl)phenyl]-6-[5-(3,5-dimethyl-1,2-oxazol-4-yl)-1-(4-methoxycyclohexyl)benzimidazol-2-yl]piperidin-2-one × 1 EDO 1,2-ETHANEDIOL × 1 NI NICKEL (II) ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1M Sodium chloride, 0.1M HEPES pH7.5, 1.6M Ammonium sulfate	Resolution 2.10 Å R-free 0.239
8FVF Bromodomain of EP300 liganded with CCS-1477 Deposited 2023-01-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1048–1161（114 aa） Fragment：bromodomain	Not recorded	JHL (6S)-1-[3,4-bis(fluoranyl)phenyl]-6-[5-(3,5-dimethyl-1,2-oxazol-4-yl)-1-(4-methoxycyclohexyl)benzimidazol-2-yl]piperidin-2-one × 1 EDO 1,2-ETHANEDIOL × 2 NI NICKEL (II) ION × 3 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1M Sodium chloride, 0.1M HEPES pH7.5, 1.6M Ammonium sulfate	Resolution 2.10 Å R-free 0.239
8GZC Crystal structure of EP300 HAT domain in complex with compound 10 Deposited 2022-09-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1159–1519（361 aa） Chain A 1581–1666（86 aa）	Mutation：Y1467E Mutation：Y1467E	ZN ZINC ION × 3 KQO (2~{R},4~{R})-4-fluoranyl-1-[1-(4-methoxyphenyl)cyclohexyl]carbonyl-~{N}-(1~{H}-pyrazolo[4,3-b]pyridin-5-yl)pyrrolidine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；15% PEG3350, 0.1 M HEPES	Resolution 2.00 Å R-free 0.227
8GZC Crystal structure of EP300 HAT domain in complex with compound 10 Deposited 2022-09-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1159–1519（361 aa） Chain B 1581–1666（86 aa）	Mutation：Y1467E Mutation：Y1467E	ZN ZINC ION × 3 KQO (2~{R},4~{R})-4-fluoranyl-1-[1-(4-methoxyphenyl)cyclohexyl]carbonyl-~{N}-(1~{H}-pyrazolo[4,3-b]pyridin-5-yl)pyrrolidine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；15% PEG3350, 0.1 M HEPES	Resolution 2.00 Å R-free 0.227
8HAG Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 1 (3.2 angstrom resolution) Deposited 2022-10-26	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 × 9 PDB declaration: undecameric	Chain K 1048–1836（789 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8HAH Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 2 (3.9 angstrom resolution) Deposited 2022-10-26	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 × 9 PDB declaration: undecameric	Chain K 1048–1836（789 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
8HAI Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 1 (4.7 angstrom resolution) Deposited 2022-10-26	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 × 9 PDB declaration: undecameric	Chain K 1048–1836（789 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.70 Å
8HAJ Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 2 (4.8 angstrom resolution) Deposited 2022-10-26	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 × 9 PDB declaration: undecameric	Chain K 1048–1836（789 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.80 Å
8HAK Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 4 (4.5 angstrom resolution) Deposited 2022-10-26	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 × 9 PDB declaration: undecameric	Chain N 1048–1836（789 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å
9IT5 p300 KAT domain in complex with KB528 Deposited 2024-07-19	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1287–1666（380 aa） Fragment：KAT domain	Mutation：K1637R/M1652G	A1L3B 4-[(2~{S})-1-[[(~{R})-[(3~{S})-7-(1-methylpyrazol-4-yl)-2,3-dihydro-1~{H}-pyrido[2,3-b][1,4]oxazin-3-yl]-phenyl-methyl]amino]propan-2-yl]benzenecarbonitrile × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；HM(PEGs-E9)-D6 (0.18M NH4Cl, 24% PEG 3350)	Resolution 2.00 Å R-free 0.238
9IT5 p300 KAT domain in complex with KB528 Deposited 2024-07-19	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1287–1666（380 aa） Fragment：KAT domain	Mutation：K1637R/M1652G	A1L3B 4-[(2~{S})-1-[[(~{R})-[(3~{S})-7-(1-methylpyrazol-4-yl)-2,3-dihydro-1~{H}-pyrido[2,3-b][1,4]oxazin-3-yl]-phenyl-methyl]amino]propan-2-yl]benzenecarbonitrile × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；HM(PEGs-E9)-D6 (0.18M NH4Cl, 24% PEG 3350)	Resolution 2.00 Å R-free 0.238
9JEJ Crystal structure of human EP300 KIX domain (L644C mutant) Deposited 2024-09-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 566–652（87 aa） Fragment：KIX domain	Mutation：L644C	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Sodium Chloride, 0.1 M Sodium Citrate : Citric Acid pH5.5, 1 M Ammonium Phosphate Dibasic	Resolution 2.90 Å R-free 0.281
9JEJ Crystal structure of human EP300 KIX domain (L644C mutant) Deposited 2024-09-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 566–652（87 aa） Fragment：KIX domain	Mutation：L644C	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Sodium Chloride, 0.1 M Sodium Citrate : Citric Acid pH5.5, 1 M Ammonium Phosphate Dibasic	Resolution 2.90 Å R-free 0.281
9JEJ Crystal structure of human EP300 KIX domain (L644C mutant) Deposited 2024-09-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 566–652（87 aa） Fragment：KIX domain	Mutation：L644C	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Sodium Chloride, 0.1 M Sodium Citrate : Citric Acid pH5.5, 1 M Ammonium Phosphate Dibasic	Resolution 2.90 Å R-free 0.281
9JUT X-ray crystal structure of Y16524 in EP300 Deposited 2024-10-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1040–1161（122 aa）	Not recorded	A1EDM (6~{S})-1-(3-chloranyl-4-methoxy-phenyl)-6-[4-(3-methyl-1,2-benzoxazol-5-yl)-1-[(2~{S})-2-morpholin-4-ylpropyl]imidazol-2-yl]piperidin-2-one × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；60% v/v Tacsimate pH 7.0, 0.1 M BIS-TRIS propane pH 7.0	Resolution 2.13 Å R-free 0.234
9MZA Chemically Hijacked BCL6-TCIP3-p300 Complex Deposited 2025-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1040–1161（122 aa） Chain D 1040–1161（122 aa）	Not recorded	A1BUC 1-{1-[5-({1-[5-chloro-4-({8-methoxy-1-methyl-3-[2-(methylamino)-2-oxoethoxy]-2-oxo-1,2-dihydroquinolin-6-yl}amino)pyrimidin-2-yl]piperidine-4-carbonyl}amino)pentanoyl]piperidin-4-yl}-3-[(6M)-7-(difluoromethyl)-6-(1-methyl-1H-pyrazol-4-yl)-3,4-dihydroquinolin-1(2H)-yl]-N-methyl-1,4,6,7-tetrahydro-5H-pyrazolo[4,3-c]pyridine-5-carboxamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；0.15 M DL-Malic acid pH 7.0, PEG 3,350 20%	Resolution 2.10 Å R-free 0.277

58 other PDB entries and 92 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	EP300_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–349； UniProt 1287–1666

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6v8b
Deposition date deposition_date	2019-12-10
Structure title title	Crystal structure of the p300 acetyltransferase domain with AcCoA competitive inhibitor 1
Keywords keywords	epigenetics, chromatin, writer, TRANSFERASE, TRANSFERASE-INHIBITOR complex; TRANSFERASE/INHIBITOR
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	21.10 Å
Radius of gyration Rg (electron density) rg_electron	19.80 Å
Forward intensity I(0) i0	22363400.00
Molecular weight molecular_weight	36478.0 kDa
Excluded volume excluded_volume	45810 Å³
Envelope volume envelope_volume	53382 Å³
Hydration-shell volume shell_volume	22230 Å³
Envelope diameter envelope_diameter	67.9 Å
Shell Rg shell_rg	26.57 Å
Envelope Rg envelope_rg	20.08 Å
Shape Rg shape_rg	19.77 Å
Total Rg total_rg	20.79 Å
Total atoms total_atoms	2570
Residues n_residues	317
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	68.1 Å
Rg (real space) rg_real	21.00 Å
Rg uncertainty (real space) rg_real_error	0.41 Å
I(0) (real space) i0_real	2.2360e+07
I(0) uncertainty (real space) i0_real_error	3.0190e+05
Rg (reciprocal space) rg_reciprocal	21.02 Å
I(0) (reciprocal space) i0_reciprocal	22360000.0000
Solution quality estimate total_estimate	0.8902
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	27.0 Å
Skewness Skewness skewness	0.225
Kurtosis Kurtosis kurtosis	-0.358
Angular range angular_range	— – 0.3750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	5852000.0000
Real-space data points n_real_points	69
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.991

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Histone acetyltransferase p300
Molecular weight formula_weight	40364.2 kDa
EC 编号 ec_number	2.3.1.48,2.3.1.-
Mutation mutation	M1652G
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2570

MKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTGCMLVELHTQSQDRF

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	4-(2-{[(1R)-2-(1H-indol-3-yl)-2-oxo-1-phenylethyl]amino}ethyl)benzene-1-sulfonamide
Molecular weight formula_weight	433.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

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8. Citations (1)

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Unit-cell length a length_a	45.782 Å
Unit-cell length b length_b	105.010 Å
Unit-cell length c length_c	168.930 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	3.130 Å
Low-resolution limit resolution_low	52.560 Å
R factor r_factor	0.2607
R_work r_work	0.2581
R_free r_free	0.3155

fit	/app/data/saxs_computation/v8/6v8b/6v8b.fit
pddf	/app/data/pr_computation/v8/6v8b/6v8b.pr.out
profile	/app/data/saxs_computation/v8/6v8b/6v8b.dat