› 1z4r

X-ray diffraction
1.74Å resolution

Human GCN5 Acetyltransferase

Released:
DOI: 10.2210/pdb1z4r/pdb
PDB entry 1z4r coloured by chain, front view.
PDB entry 1z4r coloured by chain, side view.
PDB entry 1z4r coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a binary complex between human GCN5 histone acetyltransferase domain and acetyl coenzyme A.
Schuetz A, Bernstein G, Dong A, Antoshenko T, Wu H, Loppnau P, Bochkarev A, Plotnikov AN
Proteins 68 403-7 (2007)
PMID: 17410582

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187767 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase KAT2A Chain: A
Molecule details ›
Chain: A
Length: 168 amino acids
Theoretical weight: 19.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92830 (Residues: 497-662; Coverage: 20%)
Gene names: GCN5, GCN5L2, KAT2A
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P61
Unit cell:
a: 38.09Å b: 38.09Å c: 186.34Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 0.24
Expression system: Escherichia coli

Quick links

Citations

5 review citations

NAD and ADP-ribose metabolism in mitochondria.
Dölle et al. (2013)
4 more

22 mentions without citation

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.
Ali et al. (2018)
21 more