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Crystal structure of the P300 acetyltransferase catalytic core with coenzyme a.

Analyse Crystal structure of the P300 acetyltransferase catalytic core with coenzyme a. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LKU
Type
protein
Length
551 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
COA, ZN
Pockets
7 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone acetyltransferase P300,HISTONE acetyltransferase P300 (EC 2.3.1.48)protein55140% helix, 18% strandQ09472

Ligands and binding sites

  • COA · Coenzyme A · ligand · chains A
  • ZN · Zinc ion · metal · 4 copies · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16710.740.8074COA
22450.610.8036empty
3780.500.8318empty
41220.400.7526empty
5810.370.7616empty

Compared structures

  • 5LKU · Crystal structure of the p300 acetyltransferase catalytic core with 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

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