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Human mof E350Q crystal structure with active site lysine partially acetylated

Analyse Human mof E350Q crystal structure with active site lysine partially acetylated in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TOB
Type
protein
Length
269 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone acetyltransferase MYST1
EC
2.3.1.48
UniProt
Q9H7Z6
Ligands
ZN, CL
Pockets
3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone acetyltransferase MYST1 (EC 2.3.1.48)protein26935% helix, 24% strandQ9H7Z6

Ligands and binding sites

  • ZN · Zinc ion · metal · chains A
  • CL · Chloride ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11570.670.8731empty
2630.360.7816empty
3500.310.7712empty

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

  • 3TOB · Human MOF E350Q crystal structure with active site lysine partially acetylated · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9H7Z6 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT8 (Q9H7Z6) · a predicted model of the same protein · chain A against A, TM-score 0.98

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