PDBe 1xa8

X-ray diffraction
2.4Å resolution

Crystal Structure Analysis of 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

Assemblies composition:
homo dimer (preferred)
homo tetramer
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: 100%)
Gene name: gfa
Sequence domains: Glutathione-dependent formaldehyde-activating enzyme
Structure domains: glutathione-dependent formaldehyde- activating enzyme (gfa)

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 53.91Å b: 120.62Å c: 97.14Å
α: 90° β: 97.68° γ: 90°
R-values:
R R work R free
0.199 0.195 0.248
Expression system: Escherichia coli BL21(DE3)