UniProt Q09472
Histone acetyltransferase p300 (Q09472)
Histone acetyltransferase p300 (UniProt Q09472), EC 2.3.1.-, 2.3.1.48: 93 experimental structures and 1 predicted model on GenesisL1, 30 ligands bound, 187 pockets. Binding sites, druggability and experiment against prediction…
- UniProt
- Q09472
- Protein
- Histone acetyltransferase p300
- EC
- 2.3.1.-, 2.3.1.48
- Experimental structures
- 93
- Predicted models
- 1
- Ligands
- 30
- Pockets
- 187 · 26 records with a druggable one
Structures
94 records of Q09472 in the MolNFT archive: 93 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1L3E | NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex | solution nmr | B | — | — |
| 1L3E | NMR structures of the hif-1ALPHA CTAD/P300 CH1 complex | solution nmr | B | — | — |
| 1P4Q | Solution structure of the CITED2 transactivation domain in complex with the p300 CH1 domain | solution nmr | B | — | — |
| 1P4Q | Solution structure of the CITED2 transactivation domain in complex with the P300 CH1 domain | solution nmr | B | — | — |
| 2K8F | Structural Basis for the Regulation of p53 Function by p300 | solution nmr | A | — | — |
| 2K8F | Structural basis for the regulation of P53 function by P300 | solution nmr | A | — | — |
| 2MH0 | Solution NMR structure of the p300 Taz2:ETAD1 complex | solution nmr | B | — | — |
| 2MH0 | Solution NMR structure of the P300 TAZ2:ETAD1 complex | solution nmr | B | — | — |
| 2MZD | Characterization of the p300 Taz2-p53 TAD2 Complex and Comparison with the p300 Taz2-p53 TAD1… | solution nmr | A | — | — |
| 2MZD | Characterization of the P300 TAZ2-P53 TAD2 complex and comparison with the P300 TAZ2-P53 TAD1… | solution nmr | A | — | — |
| 3BIY | Crystal structure of p300 histone acetyltransferase domain in complex with a bisubstrate inhibitor… | x-ray diffraction | A | — | — |
| 3BIY | Crystal structure of P300 histone acetyltransferase domain in complex with a bisubstrate inhibitor… | x-ray diffraction | A | — | — |
| 3I3J | Crystal Structure of the Bromodomain of Human EP300 | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | — | — |
| 3I3J | Crystal structure of the bromodomain of human EP300 | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | — | — |
| 3IO2 | Crystal structure of the Taz2 domain of p300 | x-ray diffraction | A | — | — |
| 3IO2 | Crystal structure of the TAZ2 domain of P300 | x-ray diffraction | A | — | — |
| 3P57 | Crystal structure of the p300 TAZ2 domain bound to MEF2 on DNA | x-ray diffraction | P | — | — |
| 3P57 | Crystal structure of the P300 TAZ2 domain bound to MEF2 on DNA | x-ray diffraction | P | — | — |
| 3T92 | Crystal structure of the Taz2:C/EBPepsilon-TAD chimera protein | x-ray diffraction | A | — | — |
| 3T92 | Crystal structure of the TAZ2:C/EBPEPSILON-tad chimera protein | x-ray diffraction | A | — | — |
| 4BHW | Structural basis for autoinhibition of the acetyltransferase activity of p300 | x-ray diffraction | A, B | — | — |
| 4BHW | Structural basis for autoinhibition of the acetyltransferase activity of P300 | x-ray diffraction | A, B | — | — |
| 4PZR | Crystal structure of p300 histone acetyltransferase domain in complex with Coenzyme A | x-ray diffraction | A | — | — |
| 4PZR | Crystal structure of P300 histone acetyltransferase domain in complex with coenzyme a | x-ray diffraction | A | — | — |
| 4PZS | Crystal structure of p300 histone acetyltransferase domain in complex with Acetyl-Coenzyme A | x-ray diffraction | A | — | — |
| 4PZS | Crystal structure of P300 histone acetyltransferase domain in complex with acetyl-coenzyme a | x-ray diffraction | A | — | — |
| 4PZT | Crystal structure of p300 histone acetyltransferase domain in complex with an inhibitor… | x-ray diffraction | A | — | — |
| 4PZT | Crystal structure of P300 histone acetyltransferase domain in complex with an inhibitor… | x-ray diffraction | A | — | — |
| 5BT3 | Crystal structure of EP300 bromodomain in complex with SGC-CBP30 chemical probe | x-ray diffraction | A | 2LO | 1 (best 0.47) |
| 5BT3 | Crystal structure of EP300 bromodomain in complex with sgc-CBP30 chemical probe | x-ray diffraction | A | — | — |
| 5KJ2 | The novel p300/CBP inhibitor A-485 uncovers a unique mechanism of action to target AR in castrate… | x-ray diffraction | A | 6TF, NA | 3 (best 0.76) |
| 5KJ2 | The novel P300/CBP inhibitor a-485 uncovers a unique mechanism of action to target ar in castrate… | x-ray diffraction | A | 6TF, NA | — |
| 5LKT | Crystal structure of the p300 acetyltransferase catalytic core with butyryl-coenzyme A. | x-ray diffraction | A | ZN, BCO | — |
| 5LKT | Crystal structure of the P300 acetyltransferase catalytic core with butyryl-coenzyme a. | x-ray diffraction | A | ZN, BCO | — |
| 5LKU | Crystal structure of the p300 acetyltransferase catalytic core with coenzyme A. | x-ray diffraction | A | ZN, COA | — |
| 5LKU | Crystal structure of the P300 acetyltransferase catalytic core with coenzyme a. | x-ray diffraction | A | ZN, COA | — |
| 5LKX | Crystal structure of the p300 acetyltransferase catalytic core with propionyl-coenzyme A. | x-ray diffraction | A | ZN, 1VU | 7 (best 0.73) |
| 5LKX | Crystal structure of the P300 acetyltransferase catalytic core with propionyl-coenzyme a. | x-ray diffraction | A | ZN, 1VU | — |
| 5LKZ | Crystal structure of the p300 acetyltransferase catalytic core with crotonyl-coenzyme A. | x-ray diffraction | A | ZN, COO | 8 (best 0.73) |
| 5LKZ | Crystal structure of the P300 acetyltransferase catalytic core with crotonyl-coenzyme a. | x-ray diffraction | A | ZN, COO | — |
| 5LPK | Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM1 | x-ray diffraction | A, B, C, D, E, F, G | XDM, SO4 | 12 (best 0.86) |
| 5LPK | Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM1 | x-ray diffraction | A, B, C, D, E, F, G | XDM, SO4 | — |
| 5LPM | Crystal structure of the bromodomain of human Ep300 bound to the inhibitor XDM3d | x-ray diffraction | A, B | 71Y | 4 (best 0.67) |
| 5LPM | Crystal structure of the bromodomain of human EP300 bound to the inhibitor XDM3D | x-ray diffraction | A, B | 71Y | — |
| 5NU5 | Crystal structure of the human bromodomain of EP300 bound to the inhibitor XDM-CBP | x-ray diffraction | A, B | 99E | 5 (best 0.61) |
| 5NU5 | Crystal structure of the human bromodomain of EP300 bound to the inhibitor xdm-cbp | x-ray diffraction | A, B | 99E | — |
| 5XZC | Cryo-EM structure of p300-p53 protein complex | electron microscopy | A | — | — |
| 5XZC | Cryo-EM structure of P300-P53 protein complex | electron microscopy | A | — | — |
| 6DS6 | Crystal structure of p300 ZZ domain in complex with histone H3 peptide | x-ray diffraction | A | ZN, CL | — |
| 6DS6 | Crystal structure of P300 zz domain in complex with histone H3 peptide | x-ray diffraction | A | ZN, CL | — |
| 6FGN | Solution Structure of p300Taz2-p63TA | solution nmr | A | ZN | 3 (best 0.67) |
| 6FGN | Solution structure of P300TAZ2-P63TA | solution nmr | A | ZN | — |
| 6FGS | Solution structure of p300Taz2-p73TA1 | solution nmr | A | ZN | — |
| 6FGS | Solution structure of P300TAZ2-P73TA1 | solution nmr | A | ZN | — |
| 6GYR | Transcription factor dimerization activates the p300 acetyltransferase | x-ray diffraction | A, B, C, D | ZN, 01K | 20 (best 0.81) |
| 6GYR | Transcription factor dimerization activates the P300 acetyltransferase | x-ray diffraction | A, B, C, D | ZN | — |
| 6GYT | Transcription factor dimerization activates the p300 acetyltransferase | x-ray diffraction | A, B | ZN | — |
| 6GYT | Transcription factor dimerization activates the P300 acetyltransferase | x-ray diffraction | A, B | ZN | — |
| 6K4N | Cryo-EM structure of p300 | electron microscopy | A | — | — |
| 6K4N | Cryo-EM structure of P300 | electron microscopy | A | — | — |
34 records more on the page itself.
Ligands
- ZN · Zinc ion · in 30 records
- SO4 · Sulfate ion · in 8 records
- CL · Chloride ion · in 7 records
- COA · Coenzyme A · in 7 records
- 1VU · propionyl Coenzyme A · in 2 records
- 6QI · [(6R)-6-(1H-indazol-4-ylmethyl)-1,4-oxazepan-4-yl]-[1-(4-methoxyphenyl)cyclopentyl]methanone · in 2 records
- 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 · in 2 records
- 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 · in 2 records
- 99E · ~{N}-[[2,8-bis(oxidanyl)naphthalen-1-yl]methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide · in 2 records
- BCO · Butyryl Coenzyme A · in 2 records
- COO · Crotonyl coenzyme A · in 2 records
- NA · Sodium ion · in 2 records
- OJ7 · 3-[3-chloro-5-(trifluoromethyl)pyridin-2-yl]-2-methyl-1H-indole · in 2 records
- OK7 · N-(thiophen-2-yl)acetamide · in 2 records
- QS1 · (2R)-2-{[(2S)-2-(4-cyanophenyl)propyl]amino}-N-[5-(1-methyl-1H-pyrazol-4-yl)pyridin-2-yl]-2-phenylacetamide · in 2 records
- XDM · ~{N}-[(3-chlorophenyl)methyl]-4-ethanoyl-3-ethyl-5-methyl-1~{H}-pyrrole-2-carboxamide · in 2 records
- 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 · in 2 records
- 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 · in 1 record
- 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 · in 1 record
- 6TI · (2R)-N-(2H-indazol-4-yl)-1-[1-(4-methoxyphenyl)cyclopentyl]carbonyl-pyrrolidine-2-carboxamide · in 1 record
- 6YI · (4S)-N-(3H-indazol-4-yl)-3-[1-(4-methoxyphenyl)cyclopentyl]carbonyl-1,1-bis(oxidanylidene)-1,3-thiazolidine-4-carboxamide · in 1 record
- C0C · 1-[1-(4-chlorophenyl)cyclopentane-1-carbonyl]-N-{[3-(methylcarbamoyl)phenyl]methyl}-D-prolinamide · in 1 record
- ETL · 1-[1-(4-chlorophenyl)cyclopentane-1-carbonyl]-N-1H-pyrazolo[4,3-b]pyridin-5-yl-D-prolinamide · in 1 record
- 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 · in 1 record
- 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 · in 1 record
- 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 · in 1 record
- NI · Nickel (II) ion · in 1 record
- QRY · 4-(2-{[(1R)-2-(1H-indol-3-yl)-2-oxo-1-phenylethyl]amino}ethyl)benzene-1-sulfonamide · in 1 record
- QS4 · 1-(2-methyl-1H-indol-3-yl)-2-[(2R)-2-methylpiperidin-1-yl]ethan-1-one · in 1 record
- QSD · (2R)-2-{[2-(4-cyanophenyl)ethyl]amino}-N-[5-(1-methyl-1H-pyrazol-4-yl)pyridin-2-yl]-2-phenylacetamide · in 1 record
Experiment against prediction
- 4PZR chain A against the predicted model Q09472: TM-score 1.00, RMSD 0.49 Å
- 4PZR chain A against the predicted model Q09472: TM-score 1.00, RMSD 0.49 Å
- 6PGU chain A against the predicted model Q09472: TM-score 0.99, RMSD 0.47 Å
- 6PGU chain A against the predicted model Q09472: TM-score 0.99, RMSD 0.47 Å
- 6V8K chain A against the predicted model Q09472: TM-score 0.99, RMSD 0.48 Å
- 6V8B chain A against the predicted model Q09472: TM-score 0.99, RMSD 0.52 Å
- 7SZQ chain A against the predicted model Q09472: TM-score 0.99, RMSD 0.54 Å
- 5KJ2 chain A against the predicted model Q09472: TM-score 0.99, RMSD 0.58 Å
- 5KJ2 chain A against the predicted model Q09472: TM-score 0.99, RMSD 0.58 Å
- 6PGU chain B against the predicted model Q09472: TM-score 0.99, RMSD 0.58 Å
Elsewhere
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