› 3slc

X-ray diffraction
2.7Å resolution

Crystal structure of apo form of acetate kinase (AckA) from Salmonella typhimurium

Released:
DOI: 10.2210/pdb3slc/pdb
PDB entry 3slc coloured by chain, front view.
PDB entry 3slc coloured by chain, side view.
PDB entry 3slc coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface.
Chittori S, Savithri HS, Murthy MR
BMC Struct Biol 12 24 (2012)
PMID: 23031654

Function and Biology Details

Reaction catalysed: 
ATP + acetate = ADP + acetyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159098 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetate kinase AckA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 415 amino acids
Theoretical weight: 45.06 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P63411 (Residues: 1-400; Coverage: 100%)
Gene names: STM2337, ackA
Sequence domains: Acetokinase family
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

1 bound ligand:
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: C2
Unit cell:
a: 283.159Å b: 62.168Å c: 91.695Å
α: 90° β: 93.57° γ: 90°
R-values:
R R work R free
0.224 0.221 0.283
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Protein Acetylation in Bacteria.
VanDrisse et al. (2019)
1 more

4 mentions without citation

Identification of potential drug targets by subtractive genome analysis of Escherichia coli O157:H7: an in silico approach.
Mondal et al. (2015)
3 more