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Crystal structure of the hat domain of the human moz protein

Analyse Crystal structure of the hat domain of the human moz protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2RC4
Type
protein
Length
264 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone acetyltransferase MYST3
EC
2.3.1.48, 2.3.1.-
UniProt
Q92794
Ligands
ACO, ZN
Pockets
4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone acetyltransferase MYST3 (EC 2.3.1.48, 2.3.1.-)protein26431% helix, 19% strandQ92794

Ligands and binding sites

  • ACO · Acetyl coenzyme *A · ligand · chains A
  • ZN · Zinc ion · metal · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13900.690.8153ACO
21530.620.8423empty
31230.410.7522empty
4790.400.7819empty

Compared structures

  • 2RC4 · Crystal Structure of the HAT domain of the human MOZ protein · the same entry in another collection · chain A against A, TM-score 1.00
  • Q92794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT6A (Q92794) · a predicted model of the same protein · chain A against A, TM-score 0.98

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