MolNFT v2 · #161471 · protein
Crystal structure of the p300 acetyltransferase domain with allosteric inhibitor CPI-076 and CoA
6PGU: “Crystal structure of the p300 acetyltransferase domain with allosteric inhibitor CPI-076 and CoA”. X-ray diffraction at 1.72, 2 ligands (COA, OK7). MolNFT v2 #161471 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- Q09472
- Ligands
- COA, OK7
Structure
x-ray diffraction · resolution 1.72 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 313 | — | Q09472 |
| B | — | protein | 315 | — | 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.
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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