› 2h8z

X-ray diffraction
1.42Å resolution

Xenobiotic Reductase A in complex with 8-Hydroxycoumarin

Released:
DOI: 10.2210/pdb2h8z/pdb
PDB entry 2h8z coloured by chain, front view.
PDB entry 2h8z coloured by chain, side view.
PDB entry 2h8z coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: physiological function, structure and mechanism of 8-hydroxycoumarin reduction.
Griese JJ, P Jakob R, Schwarzinger S, Dobbek H
J Mol Biol 361 140-52 (2006)
PMID: 16822524

Function and Biology Details

Reaction catalysed: 
NADPH + acceptor = NADP(+) + reduced acceptor
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183502 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH:flavin oxidoreductase/NADH oxidase N-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 359 amino acids
Theoretical weight: 39.31 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: Q88NF7 (Residues: 2-360; Coverage: 99%)
Gene names: PP_1254, xenA
Sequence domains: NADH:flavin oxidoreductase / NADH oxidase family
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
2 bound ligands:
Ligand SO4 10 x SO4
Ligand 8CM 3 x 8CM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: I222
Unit cell:
a: 57.43Å b: 83.34Å c: 156.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.202
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Microbial 2,4,6-trinitrotoluene degradation: could we learn from (bio)chemistry for bioremediation and vice versa?
Stenuit et al. (2010)
1 more