PDBe 5h84

X-ray diffraction
2Å resolution

Human Gcn5 bound to propionyl-CoA

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for acyl-group discrimination by human Gcn5L2.
OpenAccess logo Acta Crystallogr D Struct Biol 72 841-8 (2016)
PMID: 27377381

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

Structure analysis Details

Assembly composition:
monomeric (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 1VU 1 x 1VU
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P61
Unit cell:
a: 38.087Å b: 38.087Å c: 187.057Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.164 0.195
Expression system: Escherichia coli