› 4fol

X-ray diffraction
2.07Å resolution

S-formylglutathione hydrolase Variant H160I

Released:
DOI: 10.2210/pdb4fol/pdb
PDB entry 4fol coloured by chain, front view.
PDB entry 4fol coloured by chain, side view.
PDB entry 4fol coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
A role for His-160 in peroxide inhibition of S. cerevisiae S-formylglutathione hydrolase: evidence for an oxidation sensitive motif.
Legler PM, Leary DH, Hervey WJ, Millard CB
Arch Biochem Biophys 528 7-20 (2012)
PMID: 22906720

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154101 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-formylglutathione hydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 299 amino acids
Theoretical weight: 33.95 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P40363 (Residues: 1-299; Coverage: 100%)
Gene names: HRE299, J1102, YJL068C
Sequence domains: Putative esterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 66.3Å b: 119.74Å c: 169.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.283 0.281 0.327
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biological chemistry and functionality of protein sulfenic acids and related thiol modifications.
Devarie-Baez et al. (2016)
1 more

1 mention without citation

Thioesterase enzyme families: Functions, structures, and mechanisms.
Caswell et al. (2022)