› 5kf1

X-ray diffraction
2Å resolution

X-ray structure of a glucosamine N-Acetyltransferase from Clostridium acetobutylicum, apo form, pH 5

Released:
DOI: 10.2210/pdb5kf1/pdb
PDB entry 5kf1 coloured by chain, front view.
PDB entry 5kf1 coloured by chain, side view.
PDB entry 5kf1 coloured by chain, top view.
Source organism: Clostridium acetobutylicum ATCC 824
Primary publication:
Structural Studies on a Glucosamine/Glucosaminide N-Acetyltransferase.
Dopkins BJ, Tipton PA, Thoden JB, Holden HM
Biochemistry 55 4495-508 (2016)
PMID: 27348258

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188940 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 328 amino acids
Theoretical weight: 38.38 KDa
Source organism: Clostridium acetobutylicum ATCC 824
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97ML2 (Residues: 1-320; Coverage: 100%)
Gene name: CA_C0184
Sequence domains: Acetyltransferase (GNAT) family

Ligands and Environments

3 bound ligands:
Ligand ACO 2 x ACO
Ligand COA 2 x COA
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 63.864Å b: 65.694Å c: 90.486Å
α: 90° β: 106.93° γ: 90°
R-values:
R R work R free
0.187 0.184 0.238
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

An acetyltransferase effector conserved across Legionella species targets the eukaryotic eIF3 complex to modulate protein translation.
Syriste et al. (2024)

1 mention without citation

Structural Studies on a Glucosamine/Glucosaminide N-Acetyltransferase.
Dopkins et al. (2016)