› 4eqr

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
2 CoA + NADP(+) = CoA-disulfide + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173401 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coenzyme A disulfide reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 437 amino acids
Theoretical weight: 49.2 KDa
Source organism: Staphylococcus aureus subsp. aureus USA300
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2FIA5 (Residues: 2-438; Coverage: 100%)
Gene names: SAUSA300_0873, cdr
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 75.88Å b: 65.09Å c: 94.41Å
α: 90° β: 104.72° γ: 90°
R-values:
R R work R free
0.187 0.185 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Coping with inevitable accidents in metabolism.
Danchin A. (2017)
2 other articles

1 mention without citation

Turnover-dependent covalent inactivation of Staphylococcus aureus coenzyme A-disulfide reductase by coenzyme A-mimetics: mechanistic and structural insights.
Wallace et al. (2012)