MolNFT v1 · #167027 · protein
Crystal structure of the P300 acetyltransferase domain with peptide- competitive inhibitor 2
6V8K · Histone acetyltransferase P300: “Crystal structure of the P300 acetyltransferase domain with peptide- competitive inhibitor 2”. X-ray diffraction, 2 ligands (COA, QS4), 5 pockets (best druggability 0.71). MolNFT v1 #167027 on…
- PDB
- 6V8K
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase P300
- EC
- 2.3.1.48, 2.3.1.-
- UniProt
- Q09472
- Ligands
- COA, QS4
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 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 | 315 | 41% helix, 21% strand | Q09472 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
- QS4 · 1-(2-methyl-1H-indol-3-yl)-2-[(2R)-2-methylpiperidin-1-yl]ethan-1-one · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.71 | 0.83 | 47 | COA, QS4 |
| 2 | 165 | 0.58 | 0.82 | 26 | empty |
| 3 | 71 | 0.36 | 0.76 | 17 | empty |
| 4 | 75 | 0.35 | 0.76 | 15 | empty |
| 5 | 55 | 0.32 | 0.76 | 12 | empty |
Compared structures
- 6V8K · Crystal structure of the p300 acetyltransferase domain with peptide-competitive inhibitor… · 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 0.99
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 6V8K · PDBe 6V8K · UniProt Q09472
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