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4pts

X-ray diffraction
2.83Å resolution

Crystal structure of a glutathione transferase from Gordonia bronchialis DSM 43247, target EFI-507405

Released:
Model geometry
Fit model/data
Entry authors: Kim J, Toro R, Bhosle R, Al Obaidi NF, Morisco LL, Wasserman SR, Sojitra S, Attonito JD, Scott Glenn A, Chowdhury S, Evans B, Hillerich B, Love J, Seidel RD, Imker HJ, Gerlt JA, Almo SC, Enzyme Function Initiative (EFI)

Function and Biology Details

Reaction catalysed:
RX + glutathione = an S-substituted glutathione + a halide anion + H(+).
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-112002 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GST C-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 348 amino acids
Theoretical weight: 39.05 KDa
Source organism: Gordonia bronchialis DSM 43247
Expression system: Escherichia coli
UniProt:
  • Canonical: D0L9F3 (Residues: 1-348; Coverage: 100%)
Gene name: Gbro_1886
Sequence domains: Glutathione S-transferase, C-terminal domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P212121
Unit cell:
a: 52.87Å b: 75.475Å c: 193.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.248
Expression system: Escherichia coli