› 4nxy

X-ray diffraction
1.45Å resolution

Crystal Structure of the GNAT domain of S. lividans PAT

Released:
DOI: 10.2210/pdb4nxy/pdb
PDB entry 4nxy coloured by chain, front view.
PDB entry 4nxy coloured by chain, side view.
PDB entry 4nxy coloured by chain, top view.
Source organism: Streptomyces lividans TK24
Primary publication:
Insights into the specificity of lysine acetyltransferases.
Tucker AC, Taylor KC, Rank KC, Rayment I, Escalante-Semerena JC
J Biol Chem 289 36249-62 (2014)
PMID: 25381442

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164924 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-CoA synthetase Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 21.65 KDa
Source organism: Streptomyces lividans TK24
Expression system: Escherichia coli
Structure domains: Aminopeptidase

Ligands and Environments

2 bound ligands:
Ligand ETF 1 x ETF
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 40.056Å b: 56.711Å c: 74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.217
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.
Hentchel et al. (2015)
4 more

2 mentions without citation

Identification of Novel Protein Lysine Acetyltransferases in Escherichia coli.
Christensen et al. (2018)
1 more