Research workbench
Structural basis for autoinhibition of the acetyltransferase activity of p300
Analyse Structural basis for autoinhibition of the acetyltransferase activity of p300 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BHW
- Type
- protein
- Length
- 1,126 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.799
- Source
- HOMO SAPIENS
- Molecule
- Histone acetyltransferase P300
- EC
- 2.3.1.48
- UniProt
- Q09472
- Ligands
- 01K, ZN
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · resolution 2.799 · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Histone acetyltransferase P300 (EC 2.3.1.48) | protein | 563 | 40% helix, 18% strand | Q09472 |
Ligands and binding sites
- 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 · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 559 | 0.75 | 0.82 | 75 | 01K |
| 2 | 486 | 0.73 | 0.82 | 57 | 01K |
| 3 | 419 | 0.58 | 0.74 | 33 | empty |
| 4 | 194 | 0.57 | 0.80 | 32 | empty |
| 5 | 212 | 0.57 | 0.79 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 572 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 4BHW · Structural basis for autoinhibition of the acetyltransferase activity of P300 · the same entry in another collection · chain A against A, TM-score 1.00
- Q09472 · AlphaFold monomer V2.0 prediction for histone acetyltransferase P300 (Q09472) · a predicted model of the same protein · chain A against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q09472
- Elsewhere: RCSB PDB 4BHW · PDBe 4BHW · UniProt Q09472
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.