PDBe 1x6m

X-ray diffraction
2.35Å resolution

Crystal structure of the glutathione-dependent formaldehyde-activating enzyme (Gfa)

Released:
Source organism: Paracoccus denitrificans
Primary publication:
A dynamic zinc redox switch.
J. Biol. Chem. 280 2826-30 (2005)
PMID: 15548539

Function and Biology Details

Reaction catalysed:
S-(hydroxymethyl)glutathione = glutathione + formaldehyde
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione-dependent formaldehyde-activating enzyme Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 196 amino acids
Theoretical weight: 21.19 KDa
Source organism: Paracoccus denitrificans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q51669 (Residues: 2-194; Coverage: null%)
Gene name: gfa
Sequence domains: Glutathione-dependent formaldehyde-activating enzyme
Structure domains: glutathione-dependent formaldehyde- activating enzyme (gfa)

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 53.36Å b: 118.86Å c: 95.99Å
α: 90° β: 97.48° γ: 90°
R-values:
R R work R free
0.193 0.189 0.25
Expression system: Escherichia coli BL21(DE3)