PDBe 4llb

X-ray diffraction
2.5Å resolution

Crystal Structure of MOZ double PHD finger histone H3K14ac complex

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase KAT6A Chains: A, B
Molecule details ›
Chains: A, B
Length: 136 amino acids
Theoretical weight: 15.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q92794 (Residues: 194-323; Coverage: 7%)
Gene names: KAT6A, MOZ, MYST3, RUNXBP2, ZNF220
Sequence domains: PHD-finger
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)
Histone H3.1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 21 amino acids
Theoretical weight: 2.3 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: NEW P68431 (Residues: 2-22; Coverage: 15%)
Gene names: H3FA, H3FB, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3C, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: C2
Unit cell:
a: 138.63Å b: 32.23Å c: 74.73Å
α: 90° β: 94.44° γ: 90°
R-values:
R R work R free
0.222 0.219 0.266
Expression systems:
  • Escherichia coli
  • Not provided