5trl

X-ray diffraction
2.3Å resolution

Crystal structure of human GCN5 histone acetyltransferase domain

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
PDBe Complex ID:
PDB-CPX-187768 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase KAT2A Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 168 amino acids
Theoretical weight: 19.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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 SCA 8 x SCA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P213
Unit cell:
a: 175.728Å b: 175.728Å c: 175.728Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.223
Expression system: Escherichia coli BL21