PDBe 5trm

X-ray diffraction
2.9Å 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
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase KAT2A Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
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

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P41212
Unit cell:
a: 173.474Å b: 173.474Å c: 347.637Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.215 0.273
Expression system: Escherichia coli BL21