MolNFT v1 · #125836 · protein
Crystal structure of the P300 acetyltransferase catalytic core with crotonyl-coenzyme a.
5LKZ · Histone acetyltransferase P300,HISTONE acetyltransferase…: “Crystal structure of the P300 acetyltransferase catalytic core with crotonyl-coenzyme a.”. X-ray diffraction, 2 ligands (COO, ZN), 8 pockets (best druggability 0.73).…
- PDB
- 5LKZ
- Type
- protein
- Length
- 550 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
- COO, ZN
- Pockets
- 8 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase P300,HISTONE acetyltransferase P300 (EC 2.3.1.48) | protein | 550 | 41% helix, 18% strand | Q09472 |
Ligands and binding sites
- COO · Crotonyl coenzyme A · ligand · chains A
- ZN · Zinc ion · metal · 4 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 641 | 0.73 | 0.80 | 77 | COO, GOL |
| 2 | 241 | 0.60 | 0.80 | 39 | GOL |
| 3 | 115 | 0.52 | 0.81 | 20 | empty |
| 4 | 164 | 0.44 | 0.75 | 35 | empty |
| 5 | 69 | 0.40 | 0.79 | 17 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5LKZ · Crystal structure of the p300 acetyltransferase catalytic core with crotonyl-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 5LKZ · PDBe 5LKZ · UniProt Q09472
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