PDBe 1lqk

X-ray diffraction
1.35Å resolution

High Resolution Structure of Fosfomycin Resistance Protein A (FosA)

Released:

Function and Biology Details

Reaction catalysed:
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione transferase FosA Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 15.14 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9I4K6 (Residues: 1-135; Coverage: 100%)
Gene names: PA1129, fosA
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P212121
Unit cell:
a: 54.788Å b: 66.967Å c: 77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 0.137 0.177
Expression system: Escherichia coli BL21(DE3)