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 1287–1513 Chain A； UniProt 1581–1663 | 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 |
| 2 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain B； UniProt 1287–1513 Chain B； UniProt 1581–1663 | 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 |
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 6PF1 | 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 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）
|
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 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 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 |
| 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 |
| 6V8B Crystal structure of the p300 acetyltransferase domain with AcCoA competitive inhibitor 1 Deposited 2019-12-10 | 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
1287–1666（380 aa）
|
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 |
| 6V8K Crystal structure of the p300 acetyltransferase domain with peptide-competitive inhibitor 2 Deposited 2019-12-11 | Different construct 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 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）
|
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 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）
|
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 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 91 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 18–244； UniProt 1287–1513 Author chain A； PDBConstruct 256–338； UniProt 1581–1663 Author chain B； PDBConstruct 18–244； UniProt 1287–1513 Author chain B； PDBConstruct 256–338； UniProt 1581–1663 |
