PDBe 4lk9

X-ray diffraction
1.6Å resolution

Crystal Structure of MOZ double PHD finger histone H3 tail 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 Chain: A
Molecule details ›
Chain: A
Length: 136 amino acids
Theoretical weight: 15.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: 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 Chain: B
Molecule details ›
Chain: B
Length: 21 amino acids
Theoretical weight: 2.26 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: 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:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P43212
Unit cell:
a: 70.519Å b: 70.519Å c: 96.827Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.186
Expression systems:
  • Escherichia coli
  • Not provided