3s8y

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed:
S-formylglutathione + H(2)O = glutathione + formate
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-formylglutathione hydrolase Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 31.07 KDa
Source organism: Oleispira antarctica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D0VWZ4 (Residues: 1-280; Coverage: 100%)
Gene name: olei01171
Sequence domains: Putative esterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Unit cell:
a: 44.532Å b: 84.451Å c: 88.051Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.154 0.185
Expression system: Escherichia coli BL21(DE3)