3SLC

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

Summary for 3SLC

Entry DOI	10.2210/pdb3slc/pdb
Related	1G99 1SAZ 2E1Y 2IIR 3P4I 3SK3
Descriptor	Acetate kinase, 1,2-ETHANEDIOL (3 entities in total)
Functional Keywords	actin-like atpase domain, askha superfamily of phosphotransferase, acetokinase, atp binding, phosphotransferase, transferase
Biological source	Salmonella enterica subsp. enterica serovar Typhimurium
Cellular location	Cytoplasm (By similarity): P63411
Total number of polymer chains	4
Total formula weight	180473.24
Authors	Chittori, S.,Savithri, H.S.,Murthy, M.R.N. (deposition date: 2011-06-24, release date: 2012-08-29, Last modification date: 2023-11-01)
Primary citation	Chittori, S.,Savithri, H.S.,Murthy, M.R.N. Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface Bmc Struct.Biol., 12:24-24, 2012 Cited by PubMed Abstract: Bacteria such as Escherichia coli and Salmonella typhimurium can utilize acetate as the sole source of carbon and energy. Acetate kinase (AckA) and phosphotransacetylase (Pta), key enzymes of acetate utilization pathway, regulate flux of metabolites in glycolysis, gluconeogenesis, TCA cycle, glyoxylate bypass and fatty acid metabolism. PubMed: 23031654 DOI: 10.1186/1472-6807-12-24 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation