› 1pg3

X-ray diffraction
2.3Å resolution

Acetyl CoA Synthetase, Acetylated on Lys609

Released:
DOI: 10.2210/pdb1pg3/pdb
PDB entry 1pg3 coloured by chain, front view.
PDB entry 1pg3 coloured by chain, side view.
PDB entry 1pg3 coloured by chain, top view.
Source organism: Salmonella enterica
Primary publication:
The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A.
Gulick AM, Starai VJ, Horswill AR, Homick KM, Escalante-Semerena JC
Biochemistry 42 2866-73 (2003)
PMID: 12627952

Function and Biology Details

Reaction catalysed: 
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187231 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-coenzyme A synthetase Chains: A, B
Molecule details ›
Chains: A, B
Length: 652 amino acids
Theoretical weight: 72.18 KDa
Source organism: Salmonella enterica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8ZKF6 (Residues: 1-652; Coverage: 100%)
Gene names: STM4275, acs
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 2 x COA
3 bound ligands:
Ligand MG 2 x MG
Ligand PRX 2 x PRX
Ligand EDO 6 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 59.981Å b: 143.16Å c: 71.934Å
α: 90° β: 91.57° γ: 90°
R-values:
R R work R free
0.196 0.196 0.236
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

The acetate switch.
Wolfe AJ. (2005)
16 more

7 mentions without citation

Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase.
Gulick AM. (2009)
6 more