MolNFT v1 · #125834 · protein
Crystal structure of the P300 acetyltransferase catalytic core with propionyl-coenzyme a.
5LKX · Histone acetyltransferase P300,HISTONE acetyltransferase…: “Crystal structure of the P300 acetyltransferase catalytic core with propionyl-coenzyme a.”. X-ray diffraction, 2 ligands (1VU, ZN), 7 pockets (best druggability 0.73).…
- PDB
- 5LKX
- Type
- protein
- Length
- 554 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase P300,HISTONE acetyltransferase P300
- EC
- 2.3.1.48
- UniProt
- Q09472
- Ligands
- 1VU, ZN
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase P300,HISTONE acetyltransferase P300 (EC 2.3.1.48) | protein | 554 | 40% helix, 18% strand | Q09472 |
Ligands and binding sites
- 1VU · propionyl Coenzyme A · ligand · chains A
- ZN · Zinc ion · metal · 4 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 631 | 0.73 | 0.80 | 78 | 1VU, GOL |
| 2 | 255 | 0.62 | 0.80 | 33 | DMS |
| 3 | 82 | 0.45 | 0.80 | 17 | empty |
| 4 | 133 | 0.41 | 0.75 | 28 | empty |
| 5 | 63 | 0.36 | 0.78 | 16 | empty |
Compared structures
- 5LKX · Crystal structure of the p300 acetyltransferase catalytic core with propionyl-coenzyme A. · 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 0.98
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 5LKX · PDBe 5LKX · UniProt Q09472
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