› 3cw9

X-ray diffraction
2Å resolution

4-Chlorobenzoyl-CoA Ligase/Synthetase in the Thioester-forming Conformation, bound to 4-chlorophenacyl-CoA

Released:
DOI: 10.2210/pdb3cw9/pdb
PDB entry 3cw9 coloured by chain, front view.
PDB entry 3cw9 coloured by chain, side view.
PDB entry 3cw9 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 domain:

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 504 amino acids
Theoretical weight: 54.38 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


Cofactor: Ligand 01A 2 x 01A
4 bound ligands:
Ligand MG 2 x MG
Ligand NO3 3 x NO3
Ligand AMP 2 x AMP
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 60.507Å b: 87.789Å c: 186.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.209
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

14 mentions without citation

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