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Crystal structure of yeast ESA1 histone acetyltransferase domain complexed with coenzyme a

Analyse Crystal structure of yeast ESA1 histone acetyltransferase domain complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FY7
Type
protein
Length
273 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ESA1 histone acetyltransferase
UniProt
Q08649
Ligands
COA, NA
Pockets
5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AESA1 histone acetyltransferaseprotein27335% helix, 25% strandQ08649

Ligands and binding sites

  • COA · Coenzyme A · ligand · chains A
  • NA · Sodium ion · metal · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14340.700.8148NA, COA
21940.550.7927empty
3500.410.8217empty
4810.370.7718empty
5500.370.8016empty

Compared structures

  • 1FY7 · Crystal structure of yeast ESA1 histone acetyltransferase domain complexed with coenzyme a · the same entry in another collection · chain A against A, TM-score 1.00
  • Q08649 · AlphaFold monomer V2.0 prediction for histone acetyltransferase ESA1 (Q08649) · a predicted model of the same protein · chain A against A, TM-score 0.94

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