› 2qvy

X-ray diffraction
2.76Å resolution

4-Chlorobenzoyl-CoA Ligase/Synthetase, I303G mutation, bound to 3,4-Dichlorobenzoate

Released:
DOI: 10.2210/pdb2qvy/pdb
PDB entry 2qvy coloured by chain, front view.
PDB entry 2qvy coloured by chain, side view.
PDB entry 2qvy coloured by chain, top view.
Source organism: Alcaligenes sp. AL3007
Primary publication:
Rational redesign of the 4-chlorobenzoate binding site of 4-chlorobenzoate: coenzyme a ligase for expanded substrate range.
Wu R, Reger AS, Cao J, Gulick AM, Dunaway-Mariano D
Biochemistry 46 14487-99 (2007)
PMID: 18027984

Function and Biology Details

Reaction catalysed: 
4-chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184544 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-chlorobenzoyl CoA ligase Chain: X
Molecule details ›
Chain: X
Length: 504 amino acids
Theoretical weight: 54.33 KDa
Source organism: Alcaligenes sp. AL3007
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GN86 (Residues: 1-504; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 34Z 1 x 34Z
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P3221
Unit cell:
a: 127.813Å b: 127.813Å c: 71.421Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.191 0.257
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy.
Lamb AL. (2015)
9 other articles

3 mentions without citation

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