› 3cw8

X-ray diffraction
2.25Å resolution

4-Chlorobenzoyl-CoA Ligase/Synthetase, bound to 4CBA-Adenylate

Released:
DOI: 10.2210/pdb3cw8/pdb
PDB entry 3cw8 coloured by chain, front view.
PDB entry 3cw8 coloured by chain, side view.
PDB entry 3cw8 coloured by chain, top view.
Source organism: Alcaligenes sp. AL3007
Primary publication:
Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase.
Reger AS, Wu R, Dunaway-Mariano D, Gulick AM
Biochemistry 47 8016-25 (2008)
PMID: 18620418

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184543 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-chlorobenzoyl CoA ligase Chain: X
Molecule details ›
Chain: X
Length: 504 amino acids
Theoretical weight: 54.4 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

2 bound ligands:
Ligand 00A 1 x 00A
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P3221
Unit cell:
a: 128.583Å b: 128.583Å c: 72.318Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.196 0.258
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The many faces and important roles of protein-protein interactions during non-ribosomal peptide synthesis.
Izoré et al. (2018)
7 more

10 mentions without citation

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