← Back to search
6fgs

Solution structure of p300Taz2-p73TA1

Method: SOLUTION NMR Dmax: 54.7 Å Quality: GOOD
▼

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

Histone acetyltransferase p300,Tumor protein p73

Homo sapiens

UniProt O15350

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 10–31 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

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 6FGS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1COK STRUCTURE OF THE C-TERMINAL DOMAIN OF P73 Deposited 1999-05-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 439–506（68 aa） Fragment：C-TERMINAL DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 150mM NACL, 25mM SODIUM PHOSPHATE
NMR sample composition 10% WATER/90% D2O
Resolution not provided
1DXS Crystal structure of the C-terminal sterile alpha motif (SAM) domain of human p73 alpha splice variant Deposited 2000-01-15 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 487–564（78 aa） Fragment：C-TERMINAL STERILE ALPHA MOTIF (SAM) DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；CRYSTALLIZED IN 0.1M TRIS-HCL PH8.5, 2.0M MONO-AMMONIUM DIHYDROGEN PHOSPHATE, AT 290K., pH 8.50
Resolution 2.54 Å R-free 0.346
2KBY The Tetramerization Domain of Human p73 Deposited 2008-12-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Chain B 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Chain C 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Chain D 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；303 K；Pressure 1
NMR measurement conditions 303 K；Pressure 1
NMR measurement conditions pH 6.8；303 K；Pressure 1
NMR sample composition 2.5mM [U-13C; U-15N] p73 TD-1, 20mM sodium phosphate-2, 100mM sodium chloride-3, 100% D2O | 100% D2O
NMR sample composition 2.5mM [U-13C; U-15N] p73 TD-4, 20mM sodium phosphate-5, 100mM sodium chloride-6, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 2.5mM [U-15N] p73 TD-7, 20mM sodium phosphate-8, 100mM sodium chloride-9, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 2.5mM [U-15N] p73 TD-10, 2.5mM [U-13C] p73 TD-11, 20mM sodium phosphate-12, 100mM sodium chloride-13, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 2.5mM [U-15N] p73 TD-14, 2.5mM [U-13C] p73 TD-15, 20mM sodium phosphate-16, 100mM sodium chloride-17, 100% D2O | 100% D2O
NMR sample composition 2.5mM [U-10% 13C] p73 TD-18, 20mM sodium phosphate-19, 100mM sodium chloride-20, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 2.5mM [U-13C; U-15N] p73 TD-21, 16.4 Hz Pf1 phage-22, 50mM arginine-23, 50mM glutamate-24, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2MPS Structure of complex of MDM2(3-109) and P73 TAD(10-25) Deposited 2014-06-02 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 10–25（16 aa） Fragment：UNP residues 10-25
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；283 K；Ionic strength (raw mmCIF value) 50；Pressure ambient
NMR sample composition 0.9 mM [U-99% 13C; U-99% 15N] E3 Ubiquitin-protein Ligase MDM2-1, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.9 mM [U-99% 13C; U-99% 15N] Tumor protein P73-2, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2NB1 P63/p73 hetero-tetramerisation domain Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 351–398（48 aa） Fragment：Tetramerization domain of p73, UNP residues 351-398
Chain D 351–398（48 aa） Fragment：Tetramerization domain of p73, UNP residues 351-398
Mutation：E15K Mutation：E15K No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；310 K；Ionic strength (raw mmCIF value) 75；Pressure ambient
NMR measurement conditions pH 6；310 K；Ionic strength (raw mmCIF value) 5；Pressure ambient
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] p63 tetramerization domain, 0.5 mM p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5 mM p63 tetramerization domain, 0.5 mM [U-100% 13C; U-100% 15N] p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5 mM [U-100% 15N] p63 tetramerization domain, 0.5 mM [U-100% 13C] p63 tetramerization domain, 1 mM p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 1 mM p63 tetramerization domain, 0.5 mM [U-100% 15N] p73 tetramerization domain, 0.5 mM [U-100% 13C] p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5 mM [U-100% 15N] p63 tetramerization domain, 0.5 mM p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 100% D2O | 100% D2O
NMR sample composition 0.5 mM p63 tetramerization domain, 0.5 mM [U-100% 15N] p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 100% D2O | 100% D2O
NMR sample composition 0.5 mM [U-100% 15N] p63 tetramerization domain, 0.5 mM [U-100% 13C] p63 tetramerization domain, 0.5 mM [U-100% 15N] p73 tetramerization domain, 0.5 mM [U-100% 13C] p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
2WQI Crystal structure of the human p73 tetramerization domain Deposited 2009-08-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain B 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain C 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain D 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.
Resolution 1.70 Å R-free 0.254
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain H 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain I 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain J 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain K 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain L 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.
Resolution 2.00 Å R-free 0.248
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain B 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain C 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain D 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain E 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain F 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.
Resolution 2.00 Å R-free 0.248
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain S 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain T 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain U 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain V 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain W 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain X 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.
Resolution 2.00 Å R-free 0.248
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain M 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain N 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain O 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain P 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain Q 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain R 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.
Resolution 2.00 Å R-free 0.248
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain 1 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain 2 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain Y 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Chain Z 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.
Resolution 2.00 Å R-free 0.248
2WTT Structure of the human p73 tetramerization domain (crystal form II) Deposited 2009-09-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain I 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain J 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain K 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain L 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.
Resolution 2.30 Å R-free 0.287
2WTT Structure of the human p73 tetramerization domain (crystal form II) Deposited 2009-09-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain B 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain C 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain D 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.
Resolution 2.30 Å R-free 0.287
2WTT Structure of the human p73 tetramerization domain (crystal form II) Deposited 2009-09-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain F 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain G 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain H 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.
Resolution 2.30 Å R-free 0.287
2WTT Structure of the human p73 tetramerization domain (crystal form II) Deposited 2009-09-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain M 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain N 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain O 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Chain P 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.
Resolution 2.30 Å R-free 0.287
2XWC Crystal structure of the DNA binding domain of human TP73 refined at 1.8 A resolution Deposited 2010-11-03 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 112–311（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 112-311
Not recorded ZN ZINC ION × 4 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 1.2M SODIUM POTASSIUM TARTRATE, 0.25% PEG MME 5000, 0.1M TRIS PH 9
Resolution 1.82 Å R-free 0.228
3VD0 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 115–312（198 aa） Fragment：unp residue 115-312
Chain B 115–312（198 aa） Fragment：unp residue 115-312
Chain C 115–312（198 aa） Fragment：unp residue 115-312
Chain D 115–312（198 aa） Fragment：unp residue 115-312
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.1；298 K；0.1M MES, 0.1M Na acetate, pH 6.1, temperature 298.0K
Resolution 2.95 Å R-free 0.254
3VD0 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain I 115–312（198 aa） Fragment：unp residue 115-312
Chain J 115–312（198 aa） Fragment：unp residue 115-312
Chain K 115–312（198 aa） Fragment：unp residue 115-312
Chain L 115–312（198 aa） Fragment：unp residue 115-312
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.1；298 K；0.1M MES, 0.1M Na acetate, pH 6.1, temperature 298.0K
Resolution 2.95 Å R-free 0.254
3VD1 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 115–312（198 aa） Fragment：unp residue 115-312
Chain B 115–312（198 aa） Fragment：unp residue 115-312
Chain C 115–312（198 aa） Fragment：unp residue 115-312
Chain D 115–312（198 aa） Fragment：unp residue 115-312
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.1；298 K；0.1M MES, 0.1M Na acetate, pH 6.1, temperature 298.0K
Resolution 2.95 Å R-free 0.285
3VD1 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain I 115–312（198 aa） Fragment：unp residue 115-312
Chain J 115–312（198 aa） Fragment：unp residue 115-312
Chain K 115–312（198 aa） Fragment：unp residue 115-312
Chain L 115–312（198 aa） Fragment：unp residue 115-312
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.1；298 K；0.1M MES, 0.1M Na acetate, pH 6.1, temperature 298.0K
Resolution 2.95 Å R-free 0.285
3VD2 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 115–312（198 aa） Fragment：unp residues 115-312
Chain B 115–312（198 aa） Fragment：unp residues 115-312
Chain C 115–312（198 aa） Fragment：unp residues 115-312
Chain D 115–312（198 aa） Fragment：unp residues 115-312
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1M Bis-tris, 0.1M Ammonium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.5
Resolution 4.00 Å R-free 0.284
3VD2 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain I 115–312（198 aa） Fragment：unp residues 115-312
Chain J 115–312（198 aa） Fragment：unp residues 115-312
Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1M Bis-tris, 0.1M Ammonium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.5
Resolution 4.00 Å R-free 0.284
4A63 Crystal structure of the p73-ASPP2 complex at 2.6A resolution Deposited 2011-10-31 Different construct 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 112–311（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions 1.00M NA/KPO4, 0.1M ACETATE PH 4.5
Resolution 2.27 Å R-free 0.244
4A63 Crystal structure of the p73-ASPP2 complex at 2.6A resolution Deposited 2011-10-31 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 112–311（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208
Not recorded ZN ZINC ION × 1 ACT ACETATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions 1.00M NA/KPO4, 0.1M ACETATE PH 4.5
Resolution 2.27 Å R-free 0.244
4A63 Crystal structure of the p73-ASPP2 complex at 2.6A resolution Deposited 2011-10-31 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 112–311（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 1.00M NA/KPO4, 0.1M ACETATE PH 4.5
Resolution 2.27 Å R-free 0.244
4A63 Crystal structure of the p73-ASPP2 complex at 2.6A resolution Deposited 2011-10-31 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 112–311（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208
Not recorded ZN ZINC ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 1.00M NA/KPO4, 0.1M ACETATE PH 4.5
Resolution 2.27 Å R-free 0.244
4A63 Crystal structure of the p73-ASPP2 complex at 2.6A resolution Deposited 2011-10-31 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 112–311（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208
Not recorded ZN ZINC ION × 1 ACT ACETATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 1.00M NA/KPO4, 0.1M ACETATE PH 4.5
Resolution 2.27 Å R-free 0.244
4A63 Crystal structure of the p73-ASPP2 complex at 2.6A resolution Deposited 2011-10-31 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain K 112–311（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208
Not recorded ZN ZINC ION × 1 ACT ACETATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 1.00M NA/KPO4, 0.1M ACETATE PH 4.5
Resolution 2.27 Å R-free 0.244
4G82 Crystal Structure of p73 DNA-Binding Domain Tetramer bound to a Full Response-Element Deposited 2012-07-20 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 Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 115–312（198 aa） Fragment：unp residues 115-312
Chain B 115–312（198 aa） Fragment：unp residues 115-312
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9；298 K；0.1M TRIS, 20% PEG3350 , pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 3.10 Å R-free 0.268
4G83 Crystal Structure of p73 DNA-Binding Domain Tetramer bound to a Full Response-Element Deposited 2012-07-20 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 Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 115–312（198 aa）
Chain B 115–312（198 aa）
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.1M BTP, 20% PEG3350 , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 4.00 Å R-free 0.307
4GUO structure of p73 DNA binding domain complex with 12 bp DNA Deposited 2012-08-29 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 Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 115–312（198 aa） Fragment：unp residues 115-312
Chain B 115–312（198 aa） Fragment：unp residues 115-312
Chain C 115–312（198 aa） Fragment：unp residues 115-312
Chain D 115–312（198 aa） Fragment：unp residues 115-312
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6；298 K；0.1M MES, 0.1M NA ACETATE, 15-17% PEG 20K, pH 6.0, VAPOR DIFFUSION, temperature 298K
Resolution 3.19 Å R-free 0.270
4GUO structure of p73 DNA binding domain complex with 12 bp DNA Deposited 2012-08-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain I 115–312（198 aa） Fragment：unp residues 115-312
Chain J 115–312（198 aa） Fragment：unp residues 115-312
Chain K 115–312（198 aa） Fragment：unp residues 115-312
Chain L 115–312（198 aa） Fragment：unp residues 115-312
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6；298 K；0.1M MES, 0.1M NA ACETATE, 15-17% PEG 20K, pH 6.0, VAPOR DIFFUSION, temperature 298K
Resolution 3.19 Å R-free 0.270
4GUQ Structure of mutS139F p73 DNA binding domain complexed with 20BP DNA response element Deposited 2012-08-29 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 Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 115–312（198 aa） Fragment：unp residues 115-312
Chain B 115–312（198 aa） Fragment：unp residues 115-312
Mutation：S139F Mutation：S139F ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；0.1 M Tris, 50-125 mM sodium acetate and 20-24% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 3.70 Å R-free 0.316
5HOB p73 homo-tetramerization domain mutant I Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Chain B 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Chain C 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Chain D 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；15% w/v PEG Smear Medium, 0.1 M HEPES pH 7.5, 0.2 M magnesium chloride, 5 % 2-propanol, 10 % ethylene glycol
Resolution 1.22 Å R-free 0.214
5HOB p73 homo-tetramerization domain mutant I Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Chain F 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Chain G 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Chain H 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398
Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；15% w/v PEG Smear Medium, 0.1 M HEPES pH 7.5, 0.2 M magnesium chloride, 5 % 2-propanol, 10 % ethylene glycol
Resolution 1.22 Å R-free 0.214
5HOC p73 homo-tetramerization domain mutant II Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 351–398（48 aa） Fragment：UNP residues 351-398
Chain B 351–398（48 aa） Fragment：UNP residues 351-398
Mutation：E363R, K370E, E373R, R390D Mutation：E363R, K370E, E373R, R390D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；2 M Sodium chloride, 0.1 M sodium phosphate, 0.1 M potassium phosphate , 0.1 M HEPES pH 7.5
Resolution 1.36 Å R-free 0.247
5KBD Structural Studies of Transcription Factor p73 DNA Binding Domain Bound to PA26 20-mer Response Element Deposited 2016-06-03 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 Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 115–312（198 aa） Fragment：UNP residues 115-312
Chain B 115–312（198 aa） Fragment：UNP residues 115-312
Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.1 M Tris pH 9.0, 50 mM Sodium Acetate, 16% (w/v) PEG 3350; 2:1 or 4:1 Protein:DNA ratio, 1:1 protein/DNA solution:well solution ratio
Resolution 2.80 Å R-free 0.308
6IJQ Solution structure of BCL-XL bound to P73-TAD peptide Deposited 2018-10-11 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 10–25（16 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 1 mM [U-13C; U-15[U-13C; U-15N]N] Bcl-xL, 2 mM p73 peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.1 mM Bcl-XL, 1 mM p73 peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
7EZJ Crystal structure of p73 DNA binding domain complex bound with 1 bp and 2 bp spacer DNA response elements. Deposited 2021-06-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 115–312（198 aa）
Chain B 115–312（198 aa）
Chain C 115–312（198 aa）
Chain D 115–312（198 aa）
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；100 mM MES, pH-6.0, 0.1 M Ammonium acetate, 12% w/v PEg20K
Resolution 2.90 Å R-free 0.306
7EZJ Crystal structure of p73 DNA binding domain complex bound with 1 bp and 2 bp spacer DNA response elements. Deposited 2021-06-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain I 115–312（198 aa）
Chain J 115–312（198 aa）
Chain K 115–312（198 aa）
Chain L 115–312（198 aa）
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；100 mM MES, pH-6.0, 0.1 M Ammonium acetate, 12% w/v PEg20K
Resolution 2.90 Å R-free 0.306
7EZJ Crystal structure of p73 DNA binding domain complex bound with 1 bp and 2 bp spacer DNA response elements. Deposited 2021-06-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain a 115–312（198 aa）
Chain b 115–312（198 aa）
Chain c 115–312（198 aa）
Chain d 115–312（198 aa）
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；100 mM MES, pH-6.0, 0.1 M Ammonium acetate, 12% w/v PEg20K
Resolution 2.90 Å R-free 0.306
7EZJ Crystal structure of p73 DNA binding domain complex bound with 1 bp and 2 bp spacer DNA response elements. Deposited 2021-06-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain i 115–312（198 aa）
Chain j 115–312（198 aa）
Chain k 115–312（198 aa）
Chain l 115–312（198 aa）
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；100 mM MES, pH-6.0, 0.1 M Ammonium acetate, 12% w/v PEg20K
Resolution 2.90 Å R-free 0.306
8P9C Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with darpin 1810 F11 Deposited 2023-06-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain B 351–398（48 aa）
Not recorded EDO 1,2-ETHANEDIOL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；0.2M ammonium acetate, 25% PEG3350, 0.1M HEPES pH 7.5
Resolution 1.76 Å R-free 0.210
8P9D Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with darpin 1810 A2 Deposited 2023-06-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain B 351–398（48 aa）
Chain D 351–398（48 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293.15 K；20% PEG3350, 0.1M bis-tris propane pH 7.0, 0.2M salicylic, sodium salt
Resolution 2.70 Å R-free 0.252
8P9E Crystal structure of wild type p63-p73 heterotetramer (tetramerisation domain) in complex with darpin 1810 F11 Deposited 2023-06-05 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: trimeric
Chain B 351–398（48 aa）
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293.15 K；0.2M sodium chloride, 25% PEG3350, 0.1M bis-tris pH 6.5
Resolution 2.25 Å R-free 0.250
9GLQ Crystal structure of p73 tetramerisation domain in complex with darpins 1800 Deposited 2024-08-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 351–398（48 aa）
Chain B 351–398（48 aa）
Not recorded CO COBALT (II) ION × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；30% PEG2000MME, 0.15M potassium bromide
Resolution 2.10 Å R-free 0.248
9GNB Structure of p73 SAM domain in complex with DARPin B9 Deposited 2024-09-01 Different construct 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 489–550（62 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；293 K；20% PEG6000, 0.1M bicine pH 9.0
Resolution 1.80 Å R-free 0.234

27 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name P73_HUMAN
Isoform O15350-2
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 109–130； UniProt 10–31

Histone acetyltransferase p300,Tumor protein p73

Homo sapiens

UniProt Q09472

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1723–1812 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

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 6FGS 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 oligomeric state Different experimental conditions 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 oligomeric state Different experimental conditions 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 conditions 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 conditions 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 conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different experimental method 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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1723–1818（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 method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 experimental conditions 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
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 method 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 method 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 method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different experimental conditions 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 experimental conditions 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 mutation/modification Different oligomeric state Different experimental conditions 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 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 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 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 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 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 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 method 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 1–90； UniProt 1723–1812

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

SAXS profile for 6fgs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6fgs
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id6fgs
Deposition date deposition_date2018-01-11
Structure title titleSolution structure of p300Taz2-p73TA1
Keywords keywordsp300, CREB Binding protein, p53 family, p63, p73, ANTITUMOR PROTEIN; ANTITUMOR PROTEIN
Experimental Method methodSOLUTION NMR
▼

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

Radius of gyration Rg (Guinier) rg_guinier16.08 Å
Radius of gyration Rg (electron density) rg_electron15.45 Å
Forward intensity I(0) i01332850000.00
Molecular weight molecular_weight280680.0 kDa
Excluded volume excluded_volume340020 ų
Envelope volume envelope_volume47562 ų
Hydration-shell volume shell_volume20628 ų
Envelope diameter envelope_diameter63.7 Å
Shell Rg shell_rg25.85 Å
Envelope Rg envelope_rg19.59 Å
Shape Rg shape_rg15.44 Å
Total Rg total_rg15.65 Å
Total atoms total_atoms38300
Residues n_residues2600
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
▼

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

Maximum dimension Dmax dmax54.7 Å
Rg (real space) rg_real15.99 Å
Rg uncertainty (real space) rg_real_error0.35 Å
I(0) (real space) i0_real1.3330e+09
I(0) uncertainty (real space) i0_real_error1.3630e+07
Rg (reciprocal space) rg_reciprocal16.00 Å
I(0) (reciprocal space) i0_reciprocal1333000000.0000
Solution quality estimate total_estimate0.7817
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.5 Å
Skewness Skewness skewness0.162
Kurtosis Kurtosis kurtosis-0.189
Angular range angular_range— – 0.4950 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha323900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.720; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

▶

8. Citations (1)

▶

9. Files and Curves (10)