› 1yqz

X-ray diffraction
1.54Å resolution

Structure of Coenzyme A-Disulfide Reductase from Staphylococcus aureus refined at 1.54 Angstrom resolution

Released:
DOI: 10.2210/pdb1yqz/pdb
PDB entry 1yqz coloured by chain, front view.
PDB entry 1yqz coloured by chain, side view.
PDB entry 1yqz coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution.
Mallett TC, Wallen JR, Karplus PA, Sakai H, Tsukihara T, Claiborne A
Biochemistry 45 11278-89 (2006)
PMID: 16981688

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-129395 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coenzyme A disulfide reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 438 amino acids
Theoretical weight: 49.35 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O52582 (Residues: 1-438; Coverage: 100%)
Gene names: SAOUHSC_00908, cdr
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 2 x COA

Cofactor: Ligand FAD 2 x FAD
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 X26C, SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 76.06Å b: 65.2Å c: 94.49Å
α: 90° β: 104.8° γ: 90°
R-values:
R R work R free
0.18 0.177 0.206
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Glutathione analogs in prokaryotes.
Fahey RC. (2013)
3 more

8 mentions without citation

Evolution of function in the "two dinucleotide binding domains" flavoproteins.
Ojha et al. (2007)
7 more