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Crystal structure of the p300 acetyltransferase domain with allosteric inhibitor CPI-076 and CoA
Analyse Crystal structure of the p300 acetyltransferase domain with allosteric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PGU
- Type
- protein
- Length
- 628 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.72
- Source
- Homo sapiens
- Molecule
- Histone acetyltransferase p300
- EC
- 2.3.1.48, 2.3.1.-
- UniProt
- Q09472
- Ligands
- COA, OK7
- Pockets
- 10 · best druggability 0.73
Structure
x-ray diffraction · resolution 1.72 · 2 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase p300 (EC 2.3.1.48, 2.3.1.-) | protein | 313 | 41% helix, 21% strand | Q09472 |
| B | Histone acetyltransferase p300 (EC 2.3.1.48, 2.3.1.-) | protein | 315 | 40% helix, 21% strand | Q09472 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
- OK7 · N-(thiophen-2-yl)acetamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1056 | 0.73 | 0.76 | 77 | empty |
| 2 | 407 | 0.71 | 0.82 | 45 | COA |
| 3 | 283 | 0.69 | 0.84 | 34 | COA |
| 4 | 266 | 0.62 | 0.80 | 36 | OK7 |
| 5 | 210 | 0.58 | 0.80 | 33 | OK7 |
Interfaces
1 interface between chains.
- A–B · 304 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6PGU · Crystal structure of the P300 acetyltransferase domain with allosteric inhibitor cpi-076… · 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 1.00
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 6PGU · PDBe 6PGU · UniProt Q09472
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