› 4kos

X-ray diffraction
1.55Å resolution

Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with Cefmetazole

Released:
DOI: 10.2210/pdb4kos/pdb
PDB entry 4kos coloured by chain, front view.
PDB entry 4kos coloured by chain, side view.
PDB entry 4kos coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: a new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa.
Majorek KA, Kuhn ML, Chruszcz M, Anderson WF, Minor W
J Biol Chem 288 30223-30235 (2013)
PMID: 24003232

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-190989 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 18 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HV14 (Residues: 1-160; Coverage: 100%)
Gene name: PA4794
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

3 bound ligands:
Ligand 4KO 1 x 4KO
Ligand SO4 4 x SO4
Ligand EDO 12 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 57.812Å b: 76.533Å c: 39.432Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.155 0.182
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.
Favrot et al. (2016)
1 more

2 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
1 more