› 3v43

X-ray diffraction
1.47Å resolution

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159433 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase KAT6A Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92794 (Residues: 204-313; Coverage: 6%)
Gene names: KAT6A, MOZ, MYST3, RUNXBP2, ZNF220
Sequence domains: PHD-finger
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)
Histone H3.1 Chain: Q
Molecule details ›
Chain: Q
Length: 18 amino acids
Theoretical weight: 1.99 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-19; Coverage: 13%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand ACT 1 x ACT
1 modified residue:
Ligand ALY 1 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 35.08Å b: 57.63Å c: 76.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.176
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

34 review citations

The growing landscape of lysine acetylation links metabolism and cell signalling.
Choudhary et al. (2014)
33 more

6 mentions without citation

A Structural Perspective on Readout of Epigenetic Histone and DNA Methylation Marks.
Patel DJ. (2016)
5 more