2ozu

X-ray diffraction
2.3Å resolution

Crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A

Released:
Source organism: Homo sapiens
Entry authors: Min J, Wu H, Dombrovski L, Bernstein G, Dong A, Loppnau P, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Plotnikov AN, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase KAT6A Chain: A
Molecule details ›
Chain: A
Length: 284 amino acids
Theoretical weight: 33.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92794 (Residues: 497-780; Coverage: 14%)
Gene names: KAT6A, MOZ, MYST3, RUNXBP2, ZNF220
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: I222
Unit cell:
a: 58.85Å b: 104.045Å c: 109.589Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.245
Expression system: Escherichia coli BL21(DE3)