› 3e4d

X-ray diffraction
2.01Å resolution

Structural and Kinetic Study of an S-Formylglutathione Hydrolase from Agrobacterium tumefaciens

Released:
DOI: 10.2210/pdb3e4d/pdb
PDB entry 3e4d coloured by chain, front view.
PDB entry 3e4d coloured by chain, side view.
PDB entry 3e4d coloured by chain, top view.
Source organism: Agrobacterium fabrum str. C58
Primary publication:
The structure of a putative S-formylglutathione hydrolase from Agrobacterium tumefaciens.
van Straaten KE, Gonzalez CF, Valladares RB, Xu X, Savchenko AV, Sanders DA
Protein Sci 18 2196-202 (2009)
PMID: 19653299

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-108913 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-formylglutathione hydrolase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 278 amino acids
Theoretical weight: 31.92 KDa
Source organism: Agrobacterium fabrum str. C58
Expression system: Escherichia coli
UniProt:
  • Canonical: A9CJ11 (Residues: 1-277; Coverage: 100%)
Gene name: Atu1476
Sequence domains: Putative esterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand MG 6 x MG
Ligand CL 12 x CL
1 modified residue:
Ligand MSE 72 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P1
Unit cell:
a: 68.433Å b: 68.949Å c: 95.648Å
α: 92.41° β: 99.79° γ: 98.47°
R-values:
R R work R free
0.183 0.181 0.219
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Metabolic Shades of S-D-Lactoylglutathione.
Kalapos et al. (2022)
6 other articles

4 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
3 more