› 2p2q

X-ray diffraction
2.42Å resolution

Acetyl-CoA Synthetase, R584E mutation

Released:
DOI: 10.2210/pdb2p2q/pdb
PDB entry 2p2q coloured by chain, front view.
PDB entry 2p2q coloured by chain, side view.
PDB entry 2p2q coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase.
Reger AS, Carney JM, Gulick AM
Biochemistry 46 6536-46 (2007)
PMID: 17497934

Function and Biology Details

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

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: 72.21 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
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

1 bound ligand:
Ligand PRX 2 x PRX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P212121
Unit cell:
a: 92.05Å b: 95.532Å c: 164.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.184 0.245
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Explorations of catalytic domains in non-ribosomal peptide synthetase enzymology.
Hur et al. (2012)
3 more

2 mentions without citation

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