1npb

X-ray diffraction
2.5Å resolution

Crystal structure of the fosfomycin resistance protein from transposon Tn2921

Released:
Source organism: Serratia marcescens

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)
PDBe Complex ID:
PDB-CPX-176371 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione transferase FosA Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 141 amino acids
Theoretical weight: 15.97 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q56415 (Residues: 1-141; Coverage: 100%)
Gene names: fos, fosA
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: I422
Unit cell:
a: 208.597Å b: 208.597Å c: 136.358Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.23
Expression system: Escherichia coli BL21(DE3)