Uniprot accession / id : B2RWS6  OR   Uniprot accession / id : Q09472
 
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Entry Information
Entry status  (1)
REL
(58)
 
Experimental methods  (3)
X-ray diffraction
(40)
Solution NMR
(10)
Electron Microscopy
(8)
 
Authors  (363)
Suzuki T
(9)
Ortega E
(7)
Panne D
(7)
Poy F
(7)
Bommi-Reddy A
(6)
Brucelle F
(6)
Cole PA
(6)
Cummings R
(6)
Gardberg AS
(6)
Huhn AJ
(6)
Khochbin S
(6)
Marmorstein R
(6)
Vivat V
(6)
Dohmae N
(5)
Kikuchi M
(5)
Morita S
(5)
Sato S
(5)
Shin S
(5)
Shirouzu M
(5)
Uchikubo-Kamo T
(5)
Umehara T
(5)
Wakamori M
(5)
Asano M
(4)
Audia JE
(4)
Cantone N
(4)
Goudarzi A
(4)
Hanzawa H
(4)
Higuchi S
(4)
Huang H
(4)
Isoyama T
(4)
Kaczmarska Z
(4)
Kagoshima Y
(4)
Kanada R
(4)
Kihara K
(4)
Kim S
(4)
Kuroha M
(4)
Levell J
(4)
Li W
(4)
Marquez JA
(4)
Márquez JA
(4)
Naito H
(4)
Patel C
(4)
Patel G
(4)
Sato K
(4)
Sims R
(4)
Suzuki K
(4)
Takahashi M
(4)
Tominaga Y
(4)
Tropea JE
(4)
Ubukata O
(4)
Wilson JE
(4)
Zhao Y
(4)
Bai X
(3)
Banjo T
(3)
Barton L
(3)
Berrodin TJ
(3)
Boehm J
(3)
Breit B
(3)
Cecconie T
(3)
Cherry S
(3)
Di Marco C
(3)
Einsle O
(3)
Gao E
(3)
Gaucher J
(3)
Gerhardt S
(3)
Graves AP
(3)
Gunther S
(3)
Günther S
(3)
Haruta M
(3)
Hashimoto K
(3)
Hau M
(3)
Heerding D
(3)
Huegle M
(3)
Hugle M
(3)
Hügle M
(3)
Jung M
(3)
King EA
(3)
Knight S
(3)
LaFrance L
(3)
Lind K
(3)
Lucas X
(3)
Maksimoska J
(3)
Mangatt B
(3)
Martyr C
(3)
McHugh C
(3)
Medina J
(3)
Messer J
(3)
Miller M
(3)
Murata T
(3)
Nartey E
(3)
Nixon C
(3)
Obata K
(3)
Ostrovskyi D
(3)
Patel A
(3)
Phelps C
(3)
Prabhu N
(3)
Regenass P
(3)
Reid R
(3)
Reid RA
(3)
Segura-Pena D
(3)
 
More...
 
Homo / hetero assembly  (2)
homo
(41)
hetero
(16)
 
Assembly composition  (3)
protein structure
(41)
protein/protein complex
(9)
DNA/protein complex
(7)
 
Assembly polymer count  (5)
monomer
(38)
dimer
(11)
undecamer
(6)
tridecamer
(1)
trimer
(1)
 
Resolution distribution
1.0 - 1.5
(3)
1.5 - 2
(11)
2.0 - 2.5
(17)
2.5 - 3
(6)
3.0 - 3.5
(4)
3.5 - 4
(2)
4.0 - 4.5
(1)
4.5 - 5
(2)
9.5 - 10
(1)
10.5 - 11
(1)
 
Release year distribution
2000 - 2005
(2)
2005 - 2010
(4)
2010 - 2015
(9)
2015 - 2020
(23)
2020 - 2025
(26)
2025 - 2030
(1)
 
Journal  (23)
Nat Commun
(8)
Biochemistry
(6)
Bioorg Med Chem Lett
(4)
ChemMedChem
(4)
J Med Chem
(4)
Nat Chem Biol
(4)
Nature
(4)
Angew Chem Int Ed Engl
(3)
Structure
(3)
Acta Crystallogr D Biol Crystallogr
(2)
Nat Struct Mol Biol
(2)
Struct Dyn
(2)
To be published
(2)
Acta Pharmacol Sin
(1)
Biochem Biophys Res Commun
(1)
Biochim Biophys Acta Mol Cell Res
(1)
Cell
(1)
J Biol Chem
(1)
Nat Struct Biol
(1)
Nucleic Acids Res
(1)
Proc Natl Acad Sci U S A
(1)
RSC Chem Biol
(1)
iScience
(1)
 
Macromolecules
Organism superkingdom  (2)
Eukaryota
(58)
Bacteria
(1)
 
Organism name  (2)
Homo sapiens
(58)
Thermus scotoductus
(1)
 
Molecule name  (26)
E1A-associated protein p300
(58)
Histone acetyltransferase p300
(58)
Histone butyryltransferase p300
(58)
Histone crotonyltransferase p300
(58)
Protein 2-hydroxyisobutyryltransferase p300
(58)
Protein lactyltransferas p300
(58)
Protein propionyltransferase p300
(58)
p300 HAT
(58)
C/EBP epsilon
(1)
CCAAT/enhancer-binding protein epsilon
(1)
CUSP
(1)
Chronic ulcerative stomatitis protein
(1)
Keratinocyte transcription factor KET
(1)
NUT family member 1
(1)
Nuclear protein in testis
(1)
TP63
(1)
Transformation-related protein 63
(1)
Tumor protein 63
(1)
Tumor protein p73
(1)
Tumor protein p73-like
(1)
p40
(1)
p51
(1)
p53-like transcription factor
(1)
p53-related protein
(1)
p63
(1)
p73L
(1)
 
Molecule type  (1)
Protein
(58)
 
Gene names  (14)
EP300
(58)
P300
(58)
C15orf55
(1)
CEBPE
(1)
KET
(1)
NUT
(1)
NUTM1
(1)
P63
(1)
P73
(1)
P73H
(1)
P73L
(1)
TP63
(1)
TP73
(1)
TP73L
(1)
 
Interacting Molecules  (16)
Histone H4
(7)
Histone H2A type 1-B/E
(6)
Histone H2B type 1-J
(6)
Histone H3.1
(6)
DNA (180-mer)
(5)
Cbp/p300-interacting transactivator 2
(2)
Cellular tumor antigen p53
(2)
Hypoxia-inducible factor 1-alpha
(2)
DNA (145-MER)
(1)
DNA (5'-D(*A*AP*AP*CP*TP*AP*TP*TP*TP*AP*TP*AP*AP*GP*A)-3')
(1)
DNA (5'-D(*TP*TP*CP*TP*TP*AP*TP*AP*AP*AP*TP*AP*GP*TP*T)-3')
(1)
Histone acetyltransferase p300
(1)
Microphthalmia-associated transcription factor
(1)
Myocyte-specific enhancer factor 2A
(1)
NUT family member 1
(1)
Transcription factor E2-alpha
(1)
 
Interacting ligands  (44)
ZN : ZINC ION
(25)
CL : CHLORIDE ION
(6)
DMS : DIMETHYL SULFOXIDE
(6)
EDO : 1,2-ETHANEDIOL
(6)
SO4 : SULFATE ION
(6)
COA : COENZYME A
(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
(3)
GOL : GLYCEROL
(3)
ACT : ACETATE ION
(2)
PEG : DI(HYDROXYETHYL)ETHER
(2)
1VU : propionyl Coenzyme A
(1)
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)
6QI : [(6R)-6-(1H-indazol-4-ylmethyl)-1,4-oxazepan-4-yl]-[1-(4-methoxyphenyl)cyclopentyl]methanone
(1)
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)
6TI : (2R)-N-(2H-indazol-4-yl)-1-[1-(4-methoxyphenyl)cyclopentyl]carbonyl-pyrrolidine-2-carboxamide
(1)
6YI : (4S)-N-(3H-indazol-4-yl)-3-[1-(4-methoxyphenyl)cyclopentyl]carbonyl-1,1-bis(oxidanylidene)-1,3-thiazolidine-4-carboxamide
(1)
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
(1)
99E : ~{N}-[[2,8-bis(oxidanyl)naphthalen-1-yl]methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide
(1)
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)
ACO : ACETYL COENZYME *A
(1)
BCO : Butyryl Coenzyme A
(1)
C0C : 1-[1-(4-chlorophenyl)cyclopentane-1-carbonyl]-N-{[3-(methylcarbamoyl)phenyl]methyl}-D-prolinamide
(1)
C3I : N-[2-(4-methoxyanilino)-2-oxoethyl]-N-methyl-1-phenylcyclopentane-1-carboxamide
(1)
COO : CROTONYL COENZYME A
(1)
ETL : 1-[1-(4-chlorophenyl)cyclopentane-1-carbonyl]-N-1H-pyrazolo[4,3-b]pyridin-5-yl-D-prolinamide
(1)
IPA : ISOPROPYL ALCOHOL
(1)
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)
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)
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)
NA : SODIUM ION
(1)
NI : NICKEL (II) ION
(1)
OJ7 : 3-[3-chloro-5-(trifluoromethyl)pyridin-2-yl]-2-methyl-1H-indole
(1)
OK7 : N-(thiophen-2-yl)acetamide
(1)
PE5 : 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL
(1)
PG4 : TETRAETHYLENE GLYCOL
(1)
QRY : 4-(2-{[(1R)-2-(1H-indol-3-yl)-2-oxo-1-phenylethyl]amino}ethyl)benzene-1-sulfonamide
(1)
QS1 : (2R)-2-{[(2S)-2-(4-cyanophenyl)propyl]amino}-N-[5-(1-methyl-1H-pyrazol-4-yl)pyridin-2-yl]-2-phenylacetamide
(1)
QS4 : 1-(2-methyl-1H-indol-3-yl)-2-[(2R)-2-methylpiperidin-1-yl]ethan-1-one
(1)
QSD : (2R)-2-{[2-(4-cyanophenyl)ethyl]amino}-N-[5-(1-methyl-1H-pyrazol-4-yl)pyridin-2-yl]-2-phenylacetamide
(1)
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)
TAM : TRIS(HYDROXYETHYL)AMINOMETHANE
(1)
TCE : 3,3',3''-phosphanetriyltripropanoic acid
(1)
XDM : ~{N}-[(3-chlorophenyl)methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide
(1)
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)
 
Function and Biology
EC number / name  (1)
2.3.1.48 : Histone acetyltransferase
(58)
 
Biological function  (2)
histone acetyltransferase activity
(49)
zinc ion binding
(7)
 
Biological process  (1)
regulation of DNA-templated transcription
(49)
 
Compound cofactor class  (1)
Coenzyme A
(13)
 
Sequence and Structure classification
SCOP fold  (1)
TAZ domain
(2)
 
SCOP family  (1)
TAZ domain
(2)
 
CATH class  (3)
Mainly Alpha
(18)
Alpha Beta
(6)
Mainly Beta
(5)
 
CATH topology  (5)
Histone Acetyltransferase; Chain A
(10)
CREB-binding Protein; Chain A
(8)
Cysteine Rich Protein
(5)
Herpes Virus-1
(5)
Wheat Germ Agglutinin (Isolectin 2); domain 1
(1)
 
Pfam accession / name  (6)
PF08214 : HAT_KAT11
(33)
PF00439 : Bromodomain
(25)
PF06001 : RING_CBP-p300
(21)
PF02135 : zf-TAZ
(19)
PF00569 : ZZ
(7)
PF02172 : KIX
(1)
 
Experimental Information
Diffraction protocol  (2)
Single wavelength
(40)
MAD
(2)
 
Diffraction radiation source type  (2)
Synchrotron
(37)
Rotating anode
(3)
 
Diffraction source  (23)
APS BEAMLINE 22-ID
(4)
APS BEAMLINE 22-BM
(3)
ESRF BEAMLINE ID23-2
(3)
ESRF BEAMLINE ID29
(3)
NSLS BEAMLINE X6A
(3)
SLS BEAMLINE X06SA
(3)
APS BEAMLINE 17-ID
(2)
APS BEAMLINE 21-ID-D
(2)
PHOTON FACTORY BEAMLINE BL-1A
(2)
RIGAKU MICROMAX-007
(2)
ALBA BEAMLINE XALOC
(1)
ALS BEAMLINE 4.2.2
(1)
ALS BEAMLINE 8.2.1
(1)
CLSI BEAMLINE 08ID-1
(1)
DIAMOND BEAMLINE I02
(1)
DIAMOND BEAMLINE I04
(1)
ESRF BEAMLINE ID14-4
(1)
ESRF BEAMLINE ID30B
(1)
NSLS BEAMLINE X29A
(1)
PAL/PLS BEAMLINE 5C (4A)
(1)
RIGAKU MICROMAX-007 HF
(1)
SLS BEAMLINE X10SA
(1)
SSRF BEAMLINE BL02U1
(1)
 
Synchrotron site  (11)
APS
(11)
ESRF
(8)
NSLS
(4)
SLS
(4)
ALS
(2)
Diamond
(2)
Photon Factory
(2)
ALBA
(1)
CLSI
(1)
PAL/PLS
(1)
SSRF
(1)
 
Diffraction detector type  (4)
Pixel
(23)
CCD
(14)
Image plate
(2)
CMOS
(1)
 
Refinement software  (5)
PHENIX
(24)
REFMAC
(19)
phenix.real_space_refine
(5)
BUSTER
(2)
CNS
(1)
 
EM microscope model  (4)
FEI TECNAI ARCTICA
(3)
FEI POLARA 300
(2)
TFS KRIOS
(2)
FEI TITAN KRIOS
(1)
 
EM detector name  (3)
GATAN K2 SUMMIT (4k x 4k)
(3)
GATAN K3 BIOQUANTUM (6k x 4k)
(3)
FEI EAGLE (4k x 4k)
(2)
 
NMR
NMR software packages  (23)
NMRPipe
(6)
CNS
(5)
CYANA
(4)
NMRView
(4)
ARIA
(3)
CcpNmr Analysis
(2)
NMRDraw
(2)
OPAL
(2)
PROCHECK / PROCHECK-NMR
(2)
PROSA
(2)
Sparky
(2)
TALOS
(2)
TopSpin
(2)
VNMR
(2)
VnmrJ
(2)
X-PLOR
(2)
XEASY
(2)
DYANA
(1)
Insight II
(1)
MolProbity
(1)
SYBYL
(1)
Xplor-NIH
(1)
XwinNMR
(1)
 
NMR Field Strength
400.0 - 500
(5)
500.0 - 600
(10)
600.0 - 700
(8)
700.0 - 800
(9)
800.0 - 900
(5)
900.0 - 1000
(2)
 
Representative Structures
Representative Structures
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Entries 1 to 10 of 58
Entries 1 to 10 of 58
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Bromodomain of EP300 liganded with CCS-1477
Schonbrunn E, Bikowitz M
Nat Commun (2024) [PMID: 38664416  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: JHL    NI    NI    SO4    EDO   
Assembly name: Histone acetyltransferase p300 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-170794 (Preferred)   search this ID
PDBe-KB: Q09472   
X-ray diffraction
2.1Å resolution
Released: 7 Feb 2024
Model geometry
Fit model/data
8fvf
8fvf
8fvf
The novel p300/CBP inhibitor A-485 uncovers a unique mechanism of action to target AR in castrate resistant prostate cancer
Jakob CG, Qiu W, Edalji RP, Sun C
Nature (2017) [PMID: 28953875  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: 6TF    6TF    NA    NA   
Assembly name: Histone acetyltransferase p300 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-170794 (Preferred)   search this ID
PDBe-KB: Q09472   
X-ray diffraction
1.95Å resolution
Released: 27 Sep 2017
Model geometry
Fit model/data
5kj2
5kj2
5kj2
Crystal structure of the p300 acetyltransferase domain with allosteric inhibitor CPI-090 and CoA
Gardberg AS
Struct Dyn (2019) [PMID: 31649965  ]
Assembly composition: protein only structure
Bound ligands: COA    OJ7    OJ7    COA   
Assembly name: Histone acetyltransferase p300 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-170794 (Preferred)   search this ID
PDBe-KB: Q09472   
X-ray diffraction
2.32Å resolution
Released: 23 Oct 2019
Model geometry
Fit model/data
6pf1
6pf1
6pf1
Cryo-EM structure of p300-p53 protein complex
Ghosh R, Roy S, Sengupta J
Biochemistry (2019) [PMID: 31314496  ]
Source organism: Homo sapiens  
Assembly name: Cellular tumor antigen p53 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-138138 (Preferred)   search this ID
PDBe-KB: Q09472    P04637   
Electron Microscopy
10.7Å resolution
Released: 23 Jan 2019
Model geometry
Fit model/data
Data not analysed
5xzc
5xzc
5xzc
Crystal structure of the p300 acetyltransferase catalytic core with coenzyme A.
Kaczmarska Z, Ortega E, Marquez JA, Panne D
Nat Chem Biol (2017) [PMID: 27820805  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: COA    ZN    ZN    COA   
Assembly name: Histone acetyltransferase p300 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-170794 (Preferred)   search this ID
PDBe-KB: Q09472   
X-ray diffraction
3.5Å resolution
Released: 2 Nov 2016
Model geometry
Fit model/data
5lku
5lku
5lku
Crystal structure of the bromodomain of human Ep300 bound to the inhibitor XDM3d
Huegle M, Wohlwend D, Gerhardt S
Angew Chem Int Ed Engl (2017) [PMID: 28766825  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: ACT    71Y    ACT   
Assembly name: Histone acetyltransferase p300 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-170794 (Preferred)   search this ID
PDBe-KB: Q09472   
X-ray diffraction
1.5Å resolution
Released: 16 Aug 2017
Model geometry
Fit model/data
5lpm
5lpm
5lpm
Crystal structure of p300 ZZ domain in complex with histone H3 peptide
Zhang Y, Kutateladze TG
Nat Struct Mol Biol (2018) [PMID: 30150647  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: ZN    ZN    CL   
Assembly name: Histone acetyltransferase p300 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-170798 (Preferred)   search this ID
PDBe-KB: Q09472   
X-ray diffraction
1.95Å resolution
Released: 29 Aug 2018
Model geometry
Fit model/data
6ds6
6ds6
6ds6
Crystal structure of EP300 bromodomain in complex with SGC-CBP30 chemical probe
Tallant C, Hay D, Krojer T, Nunez-Alonso G, Picaud S, Newman JA, Fedorov O, von Delft F, Arrowsmith CH, Edwards AM, Bountra C, Brennan PE, Knapp S, Structural Genomics Consortium (SGC)
To be published
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: 2LO    2LO    IPA   
Assembly name: Histone acetyltransferase p300 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-170794 (Preferred)   search this ID
PDBe-KB: Q09472   
X-ray diffraction
1.05Å resolution
Released: 1 Jul 2015
Model geometry
Fit model/data
5bt3
5bt3
5bt3
Crystal structure of the p300 acetyltransferase catalytic core with crotonyl-coenzyme A.
Kaczmarska Z, Ortega E, Marquez JA, Panne D
Nat Chem Biol (2017) [PMID: 27820805  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: GOL    ZN    ZN    COO    COO   
Assembly name: Histone acetyltransferase p300 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-170794 (Preferred)   search this ID
PDBe-KB: Q09472   
X-ray diffraction
2.5Å resolution
Released: 2 Nov 2016
Model geometry
Fit model/data
5lkz
5lkz
5lkz
Crystal structure of the p300 acetyltransferase catalytic core with propionyl-coenzyme A.
Kaczmarska Z, Ortega E, Marquez JA, Panne D
Nat Chem Biol (2017) [PMID: 27820805  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: GOL    ZN    1VU    DMS    DMS    ZN    1VU   
Assembly name: Histone acetyltransferase p300 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-170794 (Preferred)   search this ID
PDBe-KB: Q09472   
X-ray diffraction
2.52Å resolution
Released: 2 Nov 2016
Model geometry
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5lkx
5lkx
5lkx
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Entries 1 to 10 of 58
Entries 1 to 10 of 58